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住友倫子

徳島大学

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2024年12月23日更新

職名: 教授
電話: 088-633-7329
電子メール: sumitomo.tomoko@tokushima-u.ac.jp
学歴: 2000/3: 徳島大学工学部生物工学科卒業
2002/3: 徳島大学大学院工学研究科生物工学専攻博士前期課程修了
2005/3: 徳島大学大学院工学研究科物質材料工学専攻博士後期課程修了
学位: 博士 (工学) (徳島大学) (2005年3月)
職歴・経歴: 2005/4: 徳島大学大学院ソシオテクノサイエンス研究部教務補佐員
2007/3: 大阪大学大学院歯学研究科口腔細菌学教室助手
2007/4: 大阪大学大学院歯学研究科口腔細菌学教室助教
2017/4: 大阪大学大学院歯学研究科口腔細菌学教室講師

専門分野・研究分野: 細菌学 (Bacteriology)
口腔細菌学 (Oral Microbiology)

研究者総覧で最新データを確認する

2024年12月23日更新

専門分野・研究分野: 細菌学 (Bacteriology)
口腔細菌学 (Oral Microbiology)
担当経験のある授業科目: 免疫学 (学部)
医用工学 (学部)
医療倫理と研究倫理 (大学院)
口腔の感染症 (学部)
口腔微生物学 (大学院)
口腔微生物学演習 (大学院)
口腔感染症学 (大学院)
基礎生物学DⅡ (共通教育)
実践口腔科学コアセミナー (大学院)
小児口腔保健学 (大学院)
微生物学・免疫学 (学部)
微生物学総論 (学部)
歯周病学概論 (大学院)
歯科衛生学臨床系基礎実習Ⅰ (学部)
病原微生物学各論 (学部)
病原微生物学実習 (学部)
総合歯科学一 (学部)
総合歯科学五 (学部)
高齢者歯科学実験実習 (大学院)
指導経験: 研究者総覧に該当データはありませんでした。

研究者総覧で最新データを確認する

2024年12月23日更新

専門分野・研究分野: 細菌学 (Bacteriology)
口腔細菌学 (Oral Microbiology)

研究テーマ: 細菌性肺炎の病態形成機構に基づく新規感染制御法の確立, 上気道定着細菌の全身伝播機構の解明 (レンサ球菌, インフルエンザウイルス, 細菌性肺炎)

著書

住友倫子, 川端重忠 :
真菌，口腔微生物学・免疫学第5版川端重忠, 小松澤均, 大原直也, 寺尾豊編,
医歯薬出版株式会社, 2021年12月. 住友倫子, 川端重忠 :
感染，イラストでわかる歯科医学の基礎第4版村上秀明, 西村康, 天野修監修,
永末書店, 2021年6月. 寺尾豊, 住友倫子, 中田匡宣, 磯田竜太朗, 川端重忠 :
病原性レンサ球菌の病原因子の機能解析，生命歯科医学のカッティング・エッジ. 米田俊之編,
大阪大学出版会, 2008年3月.

論文

Takahara Yuki, Tomoko Sumitomo, Kono Masamitsu, Takemura Moe, Akamatsu Yukako, Hirose Yujiro, Yamaguchi Masaya, Nakata Masanobu, Hotomi Muneki and Kawabata Shigetada :
Pneumolysin contributes to dysfunction of nasal epithelial barrier for promotion of pneumococcal dissemination into brain tissue,
mSphere, Vol.inpress, 2024.

(徳島大学機関リポジトリ): ● Metadata: 119623

(徳島大学機関リポジトリ: 119623) Dalia Talat, Tomoko Sumitomo, Mariko Honda-Ogawa, Yuki Takahara, Yasushi Mori, Masaya Yamaguchi, Masanobu Nakata, Madiha S Ibrahim and Shigetada Kawabata :
Two-component regulatory system TCS08 of a serotype 4 strain in pneumococcal pneumonia pathogenesis,
Journal of Oral Biosciences, Vol.66, No.3, 567-574, 2024.

(要約): Streptococcus pneumoniae, a human respiratory pathogen, causes diseases with severe morbidity and mortality rates worldwide. The two-component regulatory system (TCS) is an important signaling pathway that enables regulation of gene expression in response to environmental cues, thereby allowing an organism to adapt to a variety of host niches. Here we examined the contribution of pneumococcal TCS08 to bacterial colonization, the development of pneumonia, and pulmonary dysfunction. We employed an hk08 knockout mutant (Δhk08) with a background of the TIGR4 wild-type (WT) strain to verify whether TCS08 is associated with bacterial colonization and the development of pneumonia in a murine infection model. To clarify the association of hk08 inactivation-induced phenotypic changes with their virulence, we examined pneumococcal capsule production, colony morphology, and surface-displayed protein profiles. Pneumococcal TCS08 was involved in bacterial colonization in the respiratory tract. Interruption of the signaling pathway of TCS08 by hk08 inactivation impaired mouse survival and increased the bacterial burden within the respiratory tract. Furthermore, a histopathological examination revealed massive inflammatory cell infiltration, edema formation, and diffuse alveolar damage in the lung tissues of mice infected with Δhk08 versus the WT or complemented strain. Interestingly, virulence-associated phenotype changes, including capsule production, increased chain length, and surface-displayed protein profile, were observed in the Δhk08 strain. The present findings indicate that TCS08 contributes to pneumococcal colonization and pulmonary dysfunction by assisting adaptation to the respiratory tract milieu, leading to the development of pneumonia.
(キーワード): Animals / Pneumonia, Pneumococcal / Streptococcus pneumoniae / Mice / Virulence / Signal Transduction / Disease Models, Animal / Bacterial Proteins / Serogroup / 女性 (female)
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.job.2024.06.001
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38885903; ● Summary page in Scopus @ Elsevier: 2-s2.0-85196427975

(DOI: 10.1016/j.job.2024.06.001, PubMed: 38885903, Elsevier: Scopus) Katsuki Takebe, Mamoru Suzuki, Takeshi Sangawa, Bernd Kreikemeyer, Masaya Yamaguchi, Narikazu Uzawa, Tomoko Sumitomo, Shigetada Kawabata and Masanobu Nakata :
Analysis of FctB3 crystal structure and insight into its structural stabilization and pilin linkage mechanisms,
Archives of Microbiology, Vol.206, No.1, 4, 2023.

(要約): Streptococcus pyogenes harboring an FCT type 3 genomic region display pili composed of three types of pilins. In this study, the structure of the base pilin FctB from a serotype M3 strain (FctB3) was determined at 2.8 Å resolution. In accordance with the previously reported structure of FctB from a serotype T9 strain (FctB9), FctB3 was found to consist of an immunoglobulin-like domain and proline-rich tail region. Data obtained from structure comparison revealed main differences in the omega (Ω) loop structure and the proline-rich tail direction. In the Ω loop structure, a differential hydrogen bond network was observed, while the lysine residue responsible for linkage to growing pili was located at the same position in both structures, which indicated that switching of the hydrogen bond network in the Ω loop without changing the lysine position is advantageous for linkage to the backbone pilin FctA. The difference in direction of the proline-rich tail is potentially caused by a single residue located at the root of the proline-rich tail. Also, the FctB3 structure was found to be stabilized by intramolecular large hydrophobic interactions instead of an isopeptide bond. Comparisons of the FctB3 and FctA structures indicated that the FctA structure is more favorable for linkage to FctA. In addition, the heterodimer formation of FctB with Cpa or FctA was shown to be mediated by the putative chaperone SipA. Together, these findings provide an alternative FctB structure as well as insight into the interactions between pilin proteins.
(キーワード): Fimbriae Proteins / Lysine / Fimbriae, Bacterial / Genomics / Proline
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s00203-023-03727-1
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37994962; ● Search Scopus @ Elsevier (PMID): 37994962; ● Search Scopus @ Elsevier (DOI): 10.1007/s00203-023-03727-1

(DOI: 10.1007/s00203-023-03727-1, PubMed: 37994962) Seiko Kubota, Masanobu Nakata, Yujiro Hirose, Masaya Yamaguchi, Bernd Kreikemeyer, Narikazu Uzawa, Tomoko Sumitomo and Shigetada Kawabata :
Involvement of ribonuclease Y in pilus production by M49 Streptococcus pyogenes strain via modulation of messenger RNA level of transcriptional regulator,
Microbiology and Immunology, Vol.67, No.7, 319-333, 2023.

(要約): Streptococcus pyogenes displays a wide variety of pili, which is largely dependent on serotype. A distinct subset of S. pyogenes strains that possess the Nra transcriptional regulator demonstrates thermoregulated pilus production. Findings obtained in the present study of an Nra-positive serotype M49 strain revealed involvement of conserved virulence factor A (CvfA), also referred to as ribonuclease Y (RNase Y), in virulence factor expression and pilus production, while a cvfA deletion strain showed reduced pilus production and adherence to human keratinocytes as compared with wild-type and revertant strains. Furthermore, transcript levels of pilus subunits and srtC2 genes were decreased by cvfA deletion, which was remarkable at 25°C. Likewise, both messenger RNA (mRNA) and protein levels of Nra were remarkably decreased by cvfA deletion. Whether the expression of other pilus-related regulators, including fasX and CovR, was subject to thermoregulation was also examined. While the mRNA level of fasX, which inhibits cpa and fctA translation, was decreased by cvfA deletion at both 37°C and 25°C, CovR mRNA and protein levels, as well as its phosphorylation level were not significantly changed, suggesting that neither fasX nor CovR is necessarily involved in thermosensitive pilus production. Phenotypic analysis of the mutant strains revealed that culture temperature and cvfA deletion had varied effects on streptolysin S and SpeB activities. Furthermore, bactericidal assay data showed that cvfA deletion decreased the rate of survival in human blood. Together, the present findings indicate that CvfA is involved in regulation of pilus production and virulence-related phenotypes of the serotype M49 strain of S. pyogenes.
(キーワード): Humans / Streptococcus pyogenes / Ribonucleases / RNA, Messenger / Virulence / Virulence Factors / Bacterial Proteins / Gene Expression Regulation, Bacterial / Streptococcal Infections
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/1348-0421.13069
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37138376; ● Summary page in Scopus @ Elsevier: 2-s2.0-85158094349

(DOI: 10.1111/1348-0421.13069, PubMed: 37138376, Elsevier: Scopus) Yukako Akamatsu, Takami Akagi, Tomoko Sumitomo, Yuki Takahara, Shigehisa Akiyama, Shigetada Kawabata and Mitsuru Akashi :
Construction of human three-dimensional lung model using layer-by-layer method.,
Tissue Engineering. Part C, Methods, Vol.29, No.3, 95-102, 2023.

(要約): The respiratory tract is one of the frontline barriers for biological defense. Lung epithelial intercellular adhesions provide protection from bacterial and viral infections, and prevent invasion into deep tissues by pathogens. Dysfunction of lung epithelial intercellular adhesion caused by pathogens is associated with development of several diseases, such as acute respiratory distress syndrome (ARDS), pneumonia, and asthma. To elucidate the pathological mechanism of respiratory infections, two-dimensional cell cultures and animal models are commonly used, though are not useful for evaluating host specificity or human biological response. With the rapid progression and worldwide spread of severe acute respiratory syndrome coronavirus-2, there is increasing interest in the development of a 3D in vitro lung model for analyzing interactions between pathogens and hosts. However, some models possess unclear epithelial polarity or insufficient barrier functions, and need the use of complex technologies, have high cost, and long cultivation terms. We previously reported about the fabrication of 3D cellular multilayers using a layer-by-layer (LbL) cell coating technique with extracellular matrix protein, fibronectin (FN), and gelatin (G). In the present study, such an LbL cell coating technique was utilized to construct a human 3D lung model in which a monolayer of the human lower airway epithelial adenocarcinoma cell line Calu-3 cells was placed on 3D-cellular multilayers composed of FN-G-coated human primary pulmonary fibroblast cells. The 3D lung model thus constructed demonstrated an epithelial-fibroblast layer that maintained uniform thickness until seven days of incubation. Moreover, expressions of E-cadherin, ZO-1, and mucin in the epithelial layer were observed by immunohistochemical staining. Epithelial barrier integrity was evaluated using transepithelial electrical resistance values. The results indicate that the present constructed human 3D lung model is similar to human lung tissues, and also features epithelial polarity and a barrier function, thus is considered useful for evaluating infection and pathological mechanisms related to pneumonia and several pathogens.
(出版サイトへのリンク): ● Publication site (DOI): 10.1089/ten.TEC.2022.0184
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36721369; ● Search Scopus @ Elsevier (PMID): 36721369; ● Search Scopus @ Elsevier (DOI): 10.1089/ten.TEC.2022.0184

(DOI: 10.1089/ten.TEC.2022.0184, PubMed: 36721369) Nobuo Okahashi, Tomoko Sumitomo, Masanobu Nakata, Hirotaka Kuwata and Shigetada Kawabata :
Oral mitis group streptococci reduce infectivity of influenza A virus via acidification and H2O2 production.,
PLoS ONE, Vol.17, No.11, e0276293, 2022.

(要約): Members of the mitis group streptococci are the most abundant inhabitants of the oral cavity and dental plaque. Influenza A virus (IAV), the causative agent of influenza, infects the upper respiratory tract, and co-infection with Streptococcus pneumoniae is a major cause of morbidity during influenza epidemics. S. pneumoniae is a member of mitis group streptococci and shares many features with oral mitis group streptococci. In this study, we investigated the effect of viable Streptococcus oralis, a representative member of oral mitis group, on the infectivity of H1N1 IAV. The infectivity of IAV was measured by a plaque assay using Madin-Darby canine kidney cells. When IAV was incubated in growing culture of S. oralis, the IAV titer decreased in a time- and dose-dependent manner and became less than 100-fold, whereas heat-inactivated S. oralis had no effect. Other oral streptococci such as Streptococcus mutans and Streptococcus salivarius also reduced the viral infectivity to a lesser extent compared to S. oralis and Streptococcus gordonii, another member of the oral mitis group. S. oralis produces hydrogen peroxide (H2O2) at a concentration of 1-2 mM, and its mutant deficient in H2O2 production showed a weaker effect on the inactivation of IAV, suggesting that H2O2 contributes to viral inactivation. The contribution of H2O2 was confirmed by an inhibition assay using catalase, an H2O2-decomposing enzyme. These oral streptococci produce short chain fatty acids (SCFA) such as acetic acid as a by-product of sugar metabolism, and we also found that the inactivation of IAV was dependent on the mildly acidic pH (around pH 5.0) of these streptococcal cultures. Although inactivation of IAV in buffers of pH 5.0 was limited, incubation in the same buffer containing 2 mM H2O2 resulted in marked inactivation of IAV, which was similar to the effect of growing S. oralis culture. Taken together, these results reveal that viable S. oralis can inactivate IAV via the production of SCFAs and H2O2. This finding also suggests that the combination of mildly acidic pH and H2O2 at low concentrations could be an effective method to inactivate IAV.
(キーワード): Humans / Hydrogen Peroxide / Influenza A virus / Influenza, Human / Influenza A Virus, H1N1 Subtype / Streptococcus mitis / Streptococcus oralis / Viridans Streptococci / Streptococcus gordonii / Acids / Hydrogen-Ion Concentration
(出版サイトへのリンク): ● Publication site (DOI): 10.1371/journal.pone.0276293
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36350830; ● Search Scopus @ Elsevier (PMID): 36350830; ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0276293

(DOI: 10.1371/journal.pone.0276293, PubMed: 36350830) Bergmann René, Gulotta Giuseppe, Andreoni Federica, Tomoko Sumitomo, Kawabata Shigetada, Zinkernagel S. Annelies, Chhatwal S. Gursharan, Nizet Victor, Rohde Manfred and Uchiyama Satoshi :
The Group A Streptococcus Interleukin-8 Protease SpyCEP Promotes Bacterial Intracellular Survival by Evasion of Autophagy,
Infectious Microbes and Diseases, Vol.4, No.3, 116-123, 2022.

(出版サイトへのリンク): ● Publication site (DOI): 10.1097/IM9.0000000000000098
(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-85140002118

(DOI: 10.1097/IM9.0000000000000098, Elsevier: Scopus) Moe Takemura, Masaya Yamaguchi, Momoko Kobayashi, Tomoko Sumitomo, Yujiro Hirose, Daisuke Okuzaki, Masayuki Ono, Daisuke Motooka, Kana Goto, Masanobu Nakata, Narikazu Uzawa and Shigetada Kawabata :
Pneumococcal BgaA Promotes Host Organ Bleeding and Coagulation in a Mouse Sepsis Model.,
Frontiers in Cellular and Infection Microbiology, Vol.12, 2022.

(要約): -deleted mutant strain exhibited upregulated host innate immunity pathways, suppressed tissue damage, and blood coagulation compared with mice infected with the wild-type strain. These results suggest that BgaA functions as a multifunctional virulence factor whereby it induces host tissue damage and blood coagulation. Taken together, our results suggest that BgaA could be an attractive target for drug design and vaccine development to control pneumococcal infection.
(キーワード): Animals / Bacterial Proteins / Blood Coagulation / Disease Models, Animal / Endothelial Cells / Humans / Mice / Pneumococcal Infections / Pneumococcal Vaccines / Pneumonia, Pneumococcal / Sepsis / Streptococcus pneumoniae / Virulence Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.3389/fcimb.2022.844000
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35846740; ● Search Scopus @ Elsevier (PMID): 35846740; ● Search Scopus @ Elsevier (DOI): 10.3389/fcimb.2022.844000

(DOI: 10.3389/fcimb.2022.844000, PubMed: 35846740) Nobuo Okahashi, Tomoko Sumitomo, Masanobu Nakata and Shigetada Kawabata :
Secondary streptococcal infection following influenza.,
Microbiology and Immunology, Vol.66, No.6, 253-263, 2022.

(要約): Secondary bacterial infection following influenza type A virus (IAV) infection is a major cause of morbidity and mortality during influenza epidemics. Streptococcus pneumoniae has been identified as a predominant pathogen in secondary pneumonia cases that develop following influenza. Although IAV has been shown to enhance susceptibility to the secondary bacterial infection, the underlying mechanism of the viral-bacterial synergy leading to disease progression is complex and remains elusive. In this review, cooperative interactions of viruses and streptococci during co- or secondary infection with IAV are described. IAV infects the upper respiratory tract, therefore, streptococci that inhabit or infect the respiratory tract are of special interest. As many excellent reviews on the co-infection of IAV and S. pneumoniae have already been published, this review is intended to describe the unique interactions between other streptococci and IAV. Both streptococcal and IAV infections modulate the host epithelial barrier of the respiratory tract in various ways. IAV infection directly disrupts epithelial barriers, though at the same time the virus modifies the properties of infected cells to enhance streptococcal adherence and invasion. Mitis group streptococci produce neuraminidases, which promote IAV infection in a unique manner. The studies reviewed here have revealed intriguing mechanisms underlying secondary streptococcal infection following influenza.
(キーワード): Coinfection / Humans / Influenza A virus / Influenza, Human / Orthomyxoviridae Infections / Streptococcal Infections / Streptococcus pneumoniae
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/1348-0421.12965
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35088451; ● Search Scopus @ Elsevier (PMID): 35088451; ● Search Scopus @ Elsevier (DOI): 10.1111/1348-0421.12965

(DOI: 10.1111/1348-0421.12965, PubMed: 35088451) Tomoko Sumitomo, Masanobu Nakata, Satoshi Nagase, Yuki Takahara, Mariko Honda-Ogawa, Yasushi Mori, Yukako Akamatsu, Masaya Yamaguchi, Shigefumi Okamoto and Shigetada Kawabata :
GP96 Drives Exacerbation of Secondary Bacterial Pneumonia following Influenza A Virus Infection.,
mBio, Vol.12, No.3, 2021.

(要約): Secondary bacterial pneumonia following an influenza A virus (IAV) infection is a major cause of morbidity and mortality. Although it is generally accepted that preceding IAV infection leads to increased susceptibility to secondary bacterial infection, details regarding the pathogenic mechanism during the early stage of superinfection remain elusive. Here, we focused on the interaction of IAV-infected cells and Streptococcus pneumoniae, which revealed that human epithelial cells infected with IAV exhibit a cell surface display of GP96, an endoplasmic reticulum chaperon. Notably, extracellular GP96 was shown to impart efficient adherence for secondary infection by S. pneumoniae, and GP96 inhibition ameliorated lung pathology of superinfected mice, indicating it to be a useful target for development of therapeutic strategies for patients with superinfection.
(キーワード): A549 Cells / Animals / Bacterial Adhesion / Coinfection / Epithelial Cells / Female / Humans / Influenza A virus / Influenza, Human / Lung / Membrane Glycoproteins / Mice / Mice, Inbred BALB C / Orthomyxoviridae Infections / Pneumonia, Bacterial / Streptococcus pneumoniae / Symptom Flare Up
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/mBio.03269-20
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34061598; ● Search Scopus @ Elsevier (PMID): 34061598; ● Search Scopus @ Elsevier (DOI): 10.1128/mBio.03269-20

(DOI: 10.1128/mBio.03269-20, PubMed: 34061598) Yujiro Hirose, Masaya Yamaguchi, Tomoko Sumitomo, Masanobu Nakata, Tomoki Hanada, Daisuke Okuzaki, Daisuke Motooka, Yasushi Mori, Hiroshi Kawasaki, Alison Coady, Satoshi Uchiyama, Masanobu Hiraoka, H Raymond Zurich, Masayuki Amagai, Victor Nizet and Shigetada Kawabata :
Streptococcus pyogenes upregulates arginine catabolism to exert its pathogenesis on the skin surface.,
Cell Reports, Vol.34, No.13, 2021.

(要約): The arginine deiminase (ADI) pathway has been found in many kinds of bacteria and functions to supplement energy production and provide protection against acid stress. The Streptococcus pyogenes ADI pathway is upregulated upon exposure to various environmental stresses, including glucose starvation. However, there are several unclear points about the advantages to the organism for upregulating arginine catabolism. We show that the ADI pathway contributes to bacterial viability and pathogenesis under low-glucose conditions. S. pyogenes changes global gene expression, including upregulation of virulence genes, by catabolizing arginine. In a murine model of epicutaneous infection, S. pyogenes uses the ADI pathway to augment its pathogenicity by increasing the expression of virulence genes, including those encoding the exotoxins. We also find that arginine from stratum-corneum-derived filaggrin is a key substrate for the ADI pathway. In summary, arginine is a nutrient source that promotes the pathogenicity of S. pyogenes on the skin.
(キーワード): Animals / Arginine / Bacterial Proteins / Filaggrin Proteins / Gene Expression Regulation, Bacterial / HaCaT Cells / Humans / Hydrolases / Male / Mice, Inbred C57BL / Mice, Knockout / Microbial Viability / Phosphorylation / Skin / Streptococcal Infections / Streptococcus pyogenes / Transcriptome / Up-Regulation / Virulence
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.celrep.2021.108924
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33789094; ● Search Scopus @ Elsevier (PMID): 33789094; ● Search Scopus @ Elsevier (DOI): 10.1016/j.celrep.2021.108924

(DOI: 10.1016/j.celrep.2021.108924, PubMed: 33789094) Hirose Yujiro, Yamaguchi Masaya, Takemoto Norihiko, Miyoshi-Akiyama Tohru, Tomoko Sumitomo, Nakata Masanobu, Ikebe Tadayoshi, Hanada Tomoki, Yamaguchi Takahiro, Kawahara Ryuji, Okuno Rumi, Otsuka Hitoshi, Matsumoto Yuko, Terashima Yuji, Kazawa Yu, Nakanishi Noriko, Uchida Kaoru, Akiyama Yumi, Iwabuchi Kaori, Nakagawa Chikara, Yamamoto Kazunari, Nizet Victor and Kawabata Shigetada :
Genetic Characterization of Streptococcus pyogenes emm89 Strains Isolated in Japan From 2011 to 2019,
Infectious Microbes and Diseases, Vol.2, No.4, 160-166, 2020.

(出版サイトへのリンク): ● Publication site (DOI): 10.1097/im9.0000000000000038
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1360572092721321088; ● Search Scopus @ Elsevier (DOI): 10.1097/im9.0000000000000038

(DOI: 10.1097/im9.0000000000000038, CiNii: 1360572092721321088) Masaya Yamaguchi, Moe Takemura, Kotaro Higashi, Kana Goto, Yujiro Hirose, Tomoko Sumitomo, Masanobu Nakata, Narikazu Uzawa and Shigetada Kawabata :
Role of BgaA as a Pneumococcal Virulence Factor Elucidated by Molecular Evolutionary Analysis.,
Frontiers in Microbiology, Vol.11, 2020.

(要約): encode evolutionally conserved pneumococcal virulence factors and that molecular evolutionary analysis could be a useful alternative strategy for identification of virulence factors.
(出版サイトへのリンク): ● Publication site (DOI): 10.3389/fmicb.2020.582437
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33072054; ● Search Scopus @ Elsevier (PMID): 33072054; ● Search Scopus @ Elsevier (DOI): 10.3389/fmicb.2020.582437

(DOI: 10.3389/fmicb.2020.582437, PubMed: 33072054) Masanobu Nakata, Tomoko Sumitomo, Nadja Patenge, Bernd Kreikemeyer and Shigetada Kawabata :
Thermosensitive pilus production by FCT type 3 Streptococcus pyogenes controlled by Nra regulator translational efficiency.,
Molecular Microbiology, Vol.113, No.1, 173-189, 2019.

(要約): Streptococcus pyogenes produces a diverse variety of pili in a serotype-dependent manner and thermosensitive expression of pilus biogenesis genes was previously observed in a serotype M49 strain. However, the precise mechanism and biological significance remain unclear. Herein, the pilus expression analysis revealed the thermosensitive pilus production only in strains possessing the transcriptional regulator Nra. Experimental data obtained for nra deletion and conditional nra-expressing strains in the background of an M49 strain and the Lactococcus heterologous expression system, indicated that Nra is a positive regulator of pilus genes and also highlighted the importance of the level of intracellular Nra for the thermoregulation of pilus expression. While the nra mRNA level was not significantly influenced by a temperature shift, the Nra protein level was concomitantly increased when the culture temperature was decreased. Intriguingly, a putative stem-loop structure within the coding region of nra mRNA was a factor related to the post-transcriptional efficiency of nra mRNA translation. Either deletion of the stem-loop structure or introduction of silent chromosomal mutations designed to melt the structure attenuated Nra levels, resulting in decreased pilus production. Consequently, the temperature-dependent translational efficacy of nra mRNA influenced pilus thermoregulation, thereby potentially contributing to the fitness of nra-positive S. pyogenes in human tissues.
(キーワード): Bacterial Adhesion / Bacterial Proteins / Fimbriae, Bacterial / Gene Expression Regulation, Bacterial / Streptococcus pyogenes / Transcription Factors / Transcription, Genetic
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/mmi.14408
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31633834; ● Search Scopus @ Elsevier (PMID): 31633834; ● Search Scopus @ Elsevier (DOI): 10.1111/mmi.14408

(DOI: 10.1111/mmi.14408, PubMed: 31633834) Yujiro Hirose, Masaya Yamaguchi, Daisuke Okuzaki, Daisuke Motooka, Hiroshi Hamamoto, Tomoki Hanada, Tomoko Sumitomo, Masanobu Nakata and Shigetada Kawabata :
Streptococcus pyogenes Transcriptome Changes in the Inflammatory Environment of Necrotizing Fasciitis.,
Applied and Environmental Microbiology, Vol.85, No.21, 2019.

(要約): infection induces drastic upregulation of the expression of virulence-associated genes and shifts metabolic pathway usage. In particular, high-level expression of toxins, such as cytolysins, proteases, and nucleases, was observed at infection sites. In addition, genes identified as consistently enriched included those related to metabolism of arginine and histidine as well as carbohydrate uptake and utilization. Conversely, genes associated with the oxidative stress response and cell division were consistently downregulated during infection. The present findings provide useful information for establishing novel treatment strategies.
(キーワード): Animals / Bacterial Proteins / Cell Proliferation / Disease Models, Animal / Fasciitis, Necrotizing / Gene Expression Regulation, Bacterial / Genes, Bacterial / Host-Pathogen Interactions / Hydrolases / Male / Mice / Mice, Inbred C57BL / RNA, Bacterial / Streptococcal Infections / Streptococcus pyogenes / Streptolysins / Transcriptome / Virulence / Virulence Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/AEM.01428-19
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31471300; ● Search Scopus @ Elsevier (PMID): 31471300; ● Search Scopus @ Elsevier (DOI): 10.1128/AEM.01428-19

(DOI: 10.1128/AEM.01428-19, PubMed: 31471300) Masaya Yamaguchi, Yujiro Hirose, Moe Takemura, Masayuki Ono, Tomoko Sumitomo, Masanobu Nakata, Yutaka Terao and Shigetada Kawabata :
Evades Host Cell Phagocytosis and Limits Host Mortality Through Its Cell Wall Anchoring Protein PfbA.,
Frontiers in Cellular and Infection Microbiology, Vol.9, 2019.

(要約): species by inhibiting host cell phagocytosis, excess inflammation, and mortality by interacting with TLR2.
(キーワード): Animals / Bacterial Proteins / Bronchoalveolar Lavage Fluid / Carrier Proteins / Cell Wall / Cytophagocytosis / Disease Models, Animal / Female / HEK293 Cells / HL-60 Cells / Host-Pathogen Interactions / Humans / Immune Evasion / Inflammation / Mice / NF-kappa B / Neutrophils / Phagocytosis / Phylogeny / Pneumonia, Pneumococcal / Sepsis / Streptococcus pneumoniae / Toll-Like Receptor 2 / Toll-Like Receptor 4 / Transcriptome / Tumor Necrosis Factor-alpha
(出版サイトへのリンク): ● Publication site (DOI): 10.3389/fcimb.2019.00301
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31482074; ● Search Scopus @ Elsevier (PMID): 31482074; ● Search Scopus @ Elsevier (DOI): 10.3389/fcimb.2019.00301

(DOI: 10.3389/fcimb.2019.00301, PubMed: 31482074) Masaya Yamaguchi, Kana Goto, Yujiro Hirose, Yuka Yamaguchi, Tomoko Sumitomo, Masanobu Nakata, Kazuhiko Nakano and Shigetada Kawabata :
Identification of evolutionarily conserved virulence factor by selective pressure analysis of Streptococcus pneumoniae.,
Communications Biology, Vol.2, 96, 2019.

(要約): Evolutionarily conserved virulence factors can be candidate therapeutic targets or vaccine antigens. Here, we investigated the evolutionary selective pressures on 16 pneumococcal choline-binding cell-surface proteins since is one of the pathogens posing the greatest threats to human health. Phylogenetic and molecular analyses revealed that had the highest codon rates to total numbers of codons under considerable negative selection among those examined. Our in vitro and in vivo assays indicated that CbpJ functions as a virulence factor in pneumococcal pneumonia by contributing to evasion of neutrophil killing. Deficiency of under relaxed selective pressure also caused a similar tendency but showed no significant difference in mouse intranasal infection. Thus, molecular evolutionary analysis is a powerful tool that reveals the importance of virulence factors in real-world infection and transmission, since calculations are performed based on bacterial genome diversity following transmission of infection in an uncontrolled population.
(キーワード): Amino Acid Sequence / Bacterial Proteins / Biological Evolution / Codon / Mutation / Open Reading Frames / Phylogeny / Pneumococcal Infections / Selection, Genetic / Streptococcus pneumoniae / Virulence Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s42003-019-0340-7
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30886906; ● Search Scopus @ Elsevier (PMID): 30886906; ● Search Scopus @ Elsevier (DOI): 10.1038/s42003-019-0340-7

(DOI: 10.1038/s42003-019-0340-7, PubMed: 30886906) Tomoko Sumitomo, Yasushi Mori, Yuumi Nakamura, Mariko Honda-Ogawa, Seitaro Nakagawa, Masaya Yamaguchi, Hiroyuki Matsue, Yutaka Terao, Masanobu Nakata and Shigetada Kawabata :
Streptococcal Cysteine Protease-Mediated Cleavage of Desmogleins Is Involved in the Pathogenesis of Cutaneous Infection.,
Frontiers in Cellular and Infection Microbiology, Vol.8, 2018.

(要約): cutaneous infection.
(キーワード): Animals / Cysteine Proteases / Desmogleins / Disease Models, Animal / Humans / Mice / Mutation / Proteolysis / Skin Diseases, Bacterial / Streptococcal Infections / Streptococcus pyogenes / Virulence
(出版サイトへのリンク): ● Publication site (DOI): 10.3389/fcimb.2018.00010
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29416987; ● Search Scopus @ Elsevier (PMID): 29416987; ● Search Scopus @ Elsevier (DOI): 10.3389/fcimb.2018.00010

(DOI: 10.3389/fcimb.2018.00010, PubMed: 29416987) Yujiro Hirose, Masaya Yamaguchi, Kana Goto, Tomoko Sumitomo, Masanobu Nakata and Shigetada Kawabata :
Competence-induced protein Ccs4 facilitates pneumococcal invasion into brain tissue and virulence in meningitis.,
Virulence, Vol.9, No.1, 1576-1587, 2018.

(要約): Streptococcus pneumoniae is a major pathogen that causes pneumonia, sepsis, and meningitis. The candidate combox site 4 (ccs4) gene has been reported to be a pneumococcal competence-induced gene. Such genes are involved in development of S. pneumoniae competence and virulence, though the functions of ccs4 remain unknown. In the present study, the role of Ccs4 in the pathogenesis of pneumococcal meningitis was examined. We initially constructed a ccs4 deletion mutant and complement strains, then examined their association with and invasion into human brain microvascular endothelial cells. Wild-type and Ccs4-complemented strains exhibited significantly higher rates of association and invasion as compared to the ccs4 mutant strain. Deletion of ccs4 did not change bacterial growth activity or expression of NanA and CbpA, known brain endothelial pneumococcal adhesins. Next, mice were infected either intravenously or intranasally with pneumococcal strains. In the intranasal infection model, survival rates were comparable between wild-type strain-infected and ccs4 mutant strain-infected mice, while the ccs4 mutant strain exhibited a lower level of virulence in the intravenous infection model. In addition, at 24 hours after intravenous infection, the bacterial burden in blood was comparable between the wild-type and ccs4 mutant strain-infected mice, whereas the wild-type strain-infected mice showed a significantly higher bacterial burden in the brain. These results suggest that Ccs4 contributes to pneumococcal invasion of host brain tissues and functions as a virulence factor.
(キーワード): A549 Cells / Adhesins, Bacterial / Animals / Bacterial Load / Bacterial Proteins / Brain / Disease Models, Animal / Endothelial Cells / Female / Humans / Meningitis, Pneumococcal / Mice / Mutation / Streptococcus pneumoniae / Virulence / Virulence Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1080/21505594.2018.1526530
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30251911; ● Search Scopus @ Elsevier (PMID): 30251911; ● Search Scopus @ Elsevier (DOI): 10.1080/21505594.2018.1526530

(DOI: 10.1080/21505594.2018.1526530, PubMed: 30251911) Satoshi Nagase, Miki Matsue, Yasushi Mori, Mariko Honda-Ogawa, Kayo Sugitani, Tomoko Sumitomo, Masanobu Nakata, Shigetada Kawabata and Shigefumi Okamoto :
Comparison of antimicrobial spectrum and mechanisms of organic virgin coconut oil and lauric acid against bacteria,
Journal of Wellness and Health Care, Vol.41, No.1, 87-95, 2017.

(要約): Organic virgin coconut oil (VCO) contains almost 50% lauric acid (LA). As lauric acid exhibits antimicrobial activity against some bacteria, VCO is thought to also possess antibacterial properties. However, it is unclear whether the antimicrobial activity of VCO is comparable to that of LA. The present study was performed to examine whether VCO demonstrates antimicrobial activity against species of gram-positive bacteria (i.e., Staphylococcus aureus, Streptococcus pyogenes, Streptococcus agalactiae, Streptococcus sanguinis, Streptococcus salivarius, and Streptococcus mutans) as well as LA by disk diffusion antibacterial test. Although LA has antimicrobial activity against S. aureus, S. pyogenes, S. agalactiae, S. mutans, and S. sanguinis, VCO has antimicrobial activity against S. pyogenes, S. agalactiae, S. mutans, and S. sanguinis, but not S. aureus. Furthermore, the antimicrobial activities of VCO against several Streptococcus species were weaker than those of LA. We further compared the antimicrobial activities of VCO and LA against Streptococcus pyogenes by antimicrobial test involving the inhibition of microbial growth in broth medium. While > 4.4 mM VCO was capable of exhibiting an antimicrobial eﬀect againstS. pyogenes, the same eﬀect was demonstrated by as little as 0.18 mM LA. Furthermore, > 0.88 mM LA, but not VCO, was able to eliminate S. pyogenes completely. We also conﬁrmed thatLA could eliminate bacteria within 10 minutes, and the number of bacteria did not increasefor 2 hours. On the other hand, the addition of VCO did not decrease the number of bacteria.In addition, scanning electron microscopic (SEM) analysis indicated that the antimicrobial activity of LA is mediated by a bactericidal mechanism, whereas VCO functions by inducing bacteriostasis. Taken together, we found that VCO has antimicrobial properties against some strains of bacteria belonging to the genus Streptococcus, but not Staphylococcus aureus or some gram-negative bacteria. These ﬁndings suggest that the antimicrobial spectrum of VCO diﬀers from that of LA. We also found that the antimicrobial eﬀect of VCO is mediated by bacteriostasis, and not a bactericidal mechanism as observed for LA.
(キーワード): Organic virgin coconut oil(VCO) / Lauric acid(LA) / Streptococcus pyogenes / Antimicrobial activity / Antimicrobial mechanism
(出版サイトへのリンク): ● Publication site (DOI): 10.24517/00048862
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1390572174913608192; ● Search Scopus @ Elsevier (DOI): 10.24517/00048862

(DOI: 10.24517/00048862, CiNii: 1390572174913608192) Masaya Yamaguchi, Masanobu Nakata, Ryuichi Sumioka, Yujiro Hirose, Satoshi Wada, Yukihiro Akeda, Tomoko Sumitomo and Shigetada Kawabata :
Zinc metalloproteinase ZmpC suppresses experimental pneumococcal meningitis by inhibiting bacterial invasion of central nervous systems.,
Virulence, Vol.8, No.8, 1516-1524, 2017.

(要約): Streptococcus pneumoniae is a leading cause of bacterial meningitis. Here, we investigated whether pneumococcal paralogous zinc metalloproteases contribute to meningitis onset. Findings of codon-based phylogenetic analyses indicated 3 major clusters in the Zmp family; ZmpA, ZmpC, and ZmpB, with ZmpD as a subgroup. In vitro invasion assays of human brain microvascular endothelial cells (hBMECs) showed that deletion of the zmpC gene in S. pneumoniae strain TIGR4 significantly increased bacterial invasion into hBMECs, whereas deletion of either zmpA or zmpB had no effect. In a mouse meningitis model, the zmpC deletion mutant exhibited increased invasion of the brain and was associated with increased matrix metalloproteinase-9 in plasma and mortality as compared with the wild type. We concluded that ZmpC suppresses pneumococcal virulence by inhibiting bacterial invasion of the central nervous system. Furthermore, ZmpC illustrates the evolutional theory stating that gene duplication leads to acquisition of novel function to suppress excessive mortality.
(キーワード): Animals / Central Nervous System / Disease Models, Animal / Female / Gene Deletion / Humans / Matrix Metalloproteinase 9 / Meningitis, Pneumococcal / Metalloendopeptidases / Mice / Mice, Inbred ICR / Phylogeny / Streptococcus pneumoniae / Virulence
(出版サイトへのリンク): ● Publication site (DOI): 10.1080/21505594.2017.1328333
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28489958; ● Search Scopus @ Elsevier (PMID): 28489958; ● Search Scopus @ Elsevier (DOI): 10.1080/21505594.2017.1328333

(DOI: 10.1080/21505594.2017.1328333, PubMed: 28489958) Ryuichi Sumioka, Masanobu Nakata, Nobuo Okahashi, Yixuan Li, Satoshi Wada, Masaya Yamaguchi, Tomoko Sumitomo, Mikako Hayashi and Shigetada Kawabata :
Streptococcus sanguinis induces neutrophil cell death by production of hydrogen peroxide.,
PLoS ONE, Vol.12, No.2, 2017.

(要約): Streptococcus is the dominant bacterial genus in the human oral cavity and a leading cause of infective endocarditis. Streptococcus sanguinis belongs to the mitis group of streptococci and produces hydrogen peroxide (H2O2) by the action of SpxB, a pyruvate oxidase. In this study, we investigated the involvement of SpxB in survival of S. sanguinis in human blood and whether bacterial H2O2 exhibits cytotoxicity against human neutrophils. Results of a bactericidal test with human whole blood revealed that the spxB mutation in S. sanguinis is detrimental to its survival in blood. When S. sanguinis strains were exposed to isolated neutrophils, the bacterial survival rate was significantly decreased by spxB deletion. Furthermore, human neutrophils exposed to the S. sanguinis wild-type strain, in contrast to those exposed to an spxB mutant strain, underwent cell death with chromatin de-condensation and release of web-like extracellular DNA, reflecting induction of neutrophil extracellular traps (NETs). Since reactive oxygen species-mediated NET induction requires citrullination of arginine residues in histone proteins and subsequent chromatin de-condensation, we examined citrullination levels of histone in infected neutrophils. It is important to note that the citrullinated histone H3 was readily detected in neutrophils infected with the wild-type strain, as compared to infection with the spxB mutant strain. Moreover, decomposition of streptococcal H2O2 with catalase reduced NET induction. These results suggest that H2O2 produced by S. sanguinis provokes cell death of neutrophils and NET formation, thus potentially affecting bacterial survival in the bloodstream.
(キーワード): Adult / Bacterial Proteins / Blood Bactericidal Activity / Cell Death / Chromatin / Citrulline / Extracellular Traps / Gene Deletion / Histones / Humans / Hydrogen Peroxide / Neutrophils / Protein Processing, Post-Translational / Pyruvate Oxidase / Reactive Oxygen Species / Streptococcus sanguis / Virulence
(出版サイトへのリンク): ● Publication site (DOI): 10.1371/journal.pone.0172223
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28222125; ● Search Scopus @ Elsevier (PMID): 28222125; ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0172223

(DOI: 10.1371/journal.pone.0172223, PubMed: 28222125) Mariko Honda-Ogawa, Tomoko Sumitomo, Yasushi Mori, Talat Dalia Hamd, Taiji Ogawa, Masaya Yamaguchi, Masanobu Nakata and Shigetada Kawabata :
Endopeptidase O Contributes to Evasion from Complement-mediated Bacteriolysis via Binding to Human Complement Factor C1q.,
The Journal of Biological Chemistry, Vol.292, No.10, 4244-4254, 2017.

(要約): to evade complement-mediated bacteriolysis under acidic conditions, such as seen in inflammatory sites.
(キーワード): Animals / Bacterial Proteins / Bacteriolysis / Cell Adhesion / Cells, Cultured / Complement C1q / Endopeptidases / Enzyme-Linked Immunosorbent Assay / Female / Humans / Mice / Mice, Inbred BALB C / Pneumococcal Infections / Skin Diseases / Streptococcus pyogenes
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M116.749275
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28154192; ● Search Scopus @ Elsevier (PMID): 28154192; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M116.749275

(DOI: 10.1074/jbc.M116.749275, PubMed: 28154192) Yuichi Oogai, Masaya Yamaguchi, Miki Kawada-Matsuo, Tomoko Sumitomo, Shigetada Kawabata and Hitoshi Komatsuzawa :
Lysine and Threonine Biosynthesis from Aspartate Contributes to Staphylococcus aureus Growth in Calf Serum.,
Applied and Environmental Microbiology, Vol.82, No.20, 6150-6157, 2016.

(要約): Studying the growth of bacteria in blood is important for understanding its pathogenicity in the host. Staphylococcus aureus sometimes causes bacteremia or sepsis. However, the factors responsible for S. aureus growth in the blood are not well understood. In this study, using a library of 2,914 transposon-insertional mutants in the S. aureus MW2 strain, we identified the factors responsible for bacterial growth in CS. We found that inactivation of the lysine and threonine biosynthesis genes led to deficient growth in CS. However, the inactivation of these genes did not affect S. aureus growth in general medium. Because the concentration of amino acids in CS is low compared to that in general bacterial medium, our results suggest that lysine and threonine biosynthesis is important for the growth of S. aureus in CS. Our findings provide new insights for S. aureus adaptation in the host and for understanding the pathogenesis of bacteremia.
(キーワード): Animals / Aspartic Acid / Bacterial Proteins / Cattle / Culture Media / Lysine / Serum / Staphylococcus aureus / Threonine
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/AEM.01399-16
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27520813; ● Search Scopus @ Elsevier (PMID): 27520813; ● Search Scopus @ Elsevier (DOI): 10.1128/AEM.01399-16

(DOI: 10.1128/AEM.01399-16, PubMed: 27520813) Masaya Yamaguchi, Yujiro Hirose, Masanobu Nakata, Satoshi Uchiyama, Yuka Yamaguchi, Kana Goto, Tomoko Sumitomo, Amanda L. Lewis, Shigetada Kawabata and Victor Nizet :
Evolutionary inactivation of a sialidase in group B Streptococcus,
Scientific Reports, Vol.6, No.6, 28852, 2016.

(要約): Group B Streptococcus (GBS) is a leading cause of bacterial sepsis and meningitis in newborns. GBS possesses a protein with homology to the pneumococcal virulence factor, NanA, which has neuraminidase (sialidase) activity and promotes blood-brain barrier penetration. However, phylogenetic sequence and enzymatic analyses indicate the GBS NanA ortholog has lost sialidase function - and for this distinction we designate the gene and encoded protein nonA/NonA. Here we analyze NonA function in GBS pathogenesis, and through heterologous expression of active pneumococcal NanA in GBS, potential costs of maintaining sialidase function. GBS wild-type and ΔnonA strains lack sialidase activity, but forced expression of pneumococcal NanA in GBS induced degradation of the terminal sialic acid on its exopolysaccharide capsule. Deletion of nonA did not change GBS-whole blood survival or brain microvascular cell invasion. However, forced expression of pneumococcal NanA in GBS removed terminal sialic acid residues from the bacterial capsule, restricting bacterial proliferation in human blood and in vivo upon mouse infection. GBS expressing pneumococcal NanA had increased invasion of human brain microvascular endothelial cells. Thus, we hypothesize that nonA lost enzyme activity allowing the preservation of an effective survival factor, the sialylated exopolysaccharide capsule.
(キーワード): Animals / Bacterial Proteins / Cells, Cultured / Endothelial Cells / Evolution, Molecular / Genes, Bacterial / Humans / Mice / Microbial Viability / Neuraminidase / Phylogeny / Streptococcal Infections / Streptococcus agalactiae
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/srep28852
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27352769; ● Search Scopus @ Elsevier (PMID): 27352769; ● Search Scopus @ Elsevier (DOI): 10.1038/srep28852

(DOI: 10.1038/srep28852, PubMed: 27352769) Tomoko Sumitomo, Masanobu Nakata, Miharu Higashino, Masaya Yamaguchi and Shigetada Kawabata :
Group A Streptococcus exploits human plasminogen for bacterial translocation across epithelial barrier via tricellular tight junctions,
Scientific Reports, Vol.6, 20069, 2016.

(要約): Group A Streptococcus (GAS) is a human-specific pathogen responsible for local suppurative and life-threatening invasive systemic diseases. Interaction of GAS with human plasminogen (PLG) is a salient characteristic for promoting their systemic dissemination. In the present study, a serotype M28 strain was found predominantly localized in tricellular tight junctions of epithelial cells cultured in the presence of PLG. Several lines of evidence indicated that interaction of PLG with tricellulin, a major component of tricellular tight junctions, is crucial for bacterial localization. A site-directed mutagenesis approach revealed that lysine residues at positions 217 and 252 within the extracellular loop of tricellulin play important roles in PLG-binding activity. Additionally, we demonstrated that PLG functions as a molecular bridge between tricellulin and streptococcal surface enolase (SEN). The wild type strain efficiently translocated across the epithelial monolayer, accompanied by cleavage of transmembrane junctional proteins. In contrast, amino acid substitutions in the PLG-binding motif of SEN markedly compromised those activities. Notably, the interaction of PLG with SEN was dependent on PLG species specificity, which influenced the efficiency of bacterial penetration. Our findings provide insight into the mechanism by which GAS exploits host PLG for acceleration of bacterial invasion into deeper tissues via tricellular tight junctions.
(キーワード): Bacterial Proteins / Bacterial Translocation / Caco-2 Cells / Carrier Proteins / Epithelial Cells / Host-Pathogen Interactions / Humans / MARVEL Domain Containing 2 Protein / Mutagenesis, Site-Directed / Phosphopyruvate Hydratase / Plasminogen / Species Specificity / Streptococcus pyogenes / Surface Plasmon Resonance / Tight Junctions
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/srep20069
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26822058; ● Search Scopus @ Elsevier (PMID): 26822058; ● Search Scopus @ Elsevier (DOI): 10.1038/srep20069

(DOI: 10.1038/srep20069, PubMed: 26822058) Tomoko Sumitomo :
Group A Streptococcus translocates across an epithelial barrier via degradation of intercellular junctions,
Journal of Oral Biosciences, Vol.57, No.3, 135-138, 2015. Chisato Morita, Ryuichi Sumioka, Masanobu Nakata, Nobuo Okahashi, Satoshi Wada, Takashi Yamashiro, Mikako Hayashi, Shigeyuki Hamada, Tomoko Sumitomo and Shigetada Kawabata :
Cell wall-anchored nuclease of Streptococcus sanguinis contributes to escape from neutrophil extracellular trap-mediated bacteriocidal activity.,
PLoS ONE, Vol.9, No.8, e103125, 2014.

(要約): Streptococcus sanguinis, a member of the commensal mitis group of streptococci, is a primary colonizer of the tooth surface, and has been implicated in infectious complications including bacteremia and infective endocarditis. During disease progression, S. sanguinis may utilize various cell surface molecules to evade the host immune system to survive in blood. In the present study, we discovered a novel cell surface nuclease with a cell-wall anchor domain, termed SWAN (streptococcal wall-anchored nuclease), and investigated its contribution to bacterial resistance against the bacteriocidal activity of neutrophil extracellular traps (NETs). Recombinant SWAN protein (rSWAN) digested multiple forms of DNA including NET DNA and human RNA, which required both Mg(2+) and Ca(2+) for optimum activity. Furthermore, DNase activity of S. sanguinis was detected around growing colonies on agar plates containing DNA. In-frame deletion of the swan gene mostly reduced that activity. These findings indicated that SWAN is a major nuclease displayed on the surface, which was further confirmed by immuno-detection of SWAN in the cell wall fraction. The sensitivity of S. sanguinis to NET killing was reduced by swan gene deletion. Moreover, heterologous expression of the swan gene rendered a Lactococcus lactis strain more resistant to NET killing. Our results suggest that the SWAN nuclease on the bacterial surface contributes to survival in the potential situation of S. sanguinis encountering NETs during the course of disease progression.
(キーワード): Cell Wall / DNA, Viral / Enzyme Activation / Extracellular Space / Extracellular Traps / Gene Order / Genetic Loci / Humans / Hydrolysis / Micrococcal Nuclease / Neutrophils / Protein Transport / RNA, Viral / Recombinant Fusion Proteins / Streptococcus sanguis
(出版サイトへのリンク): ● Publication site (DOI): 10.1371/journal.pone.0103125
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25084357; ● Search Scopus @ Elsevier (PMID): 25084357; ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0103125

(DOI: 10.1371/journal.pone.0103125, PubMed: 25084357) Nobuo Okahashi, Tomoko Sumitomo, Masanobu Nakata, Atsuo Sakurai, Hirotaka Kuwata and Shigetada Kawabata :
Hydrogen peroxide contributes to the epithelial cell death induced by the oral mitis group of streptococci.,
PLoS ONE, Vol.9, No.1, 2014.

(要約): Members of the mitis group of streptococci are normal inhabitants of the commensal flora of the oral cavity and upper respiratory tract of humans. Some mitis group species, such as Streptococcus oralis and Streptococcus sanguinis, are primary colonizers of the human oral cavity. Recently, we found that hydrogen peroxide (H2O2) produced by S. oralis is cytotoxic to human macrophages, suggesting that streptococcus-derived H2O2 may act as a cytotoxin. Since epithelial cells provide a physical barrier against pathogenic microbes, we investigated their susceptibility to infection by H2O2-producing streptococci in this study. Infection by S. oralis and S. sanguinis was found to stimulate cell death of Detroit 562, Calu-3 and HeLa epithelial cell lines at a multiplicity of infection greater than 100. Catalase, an enzyme that catalyzes the decomposition of H2O2, inhibited S. oralis cytotoxicity, and H2O2 alone was capable of eliciting epithelial cell death. Moreover, S. oralis mutants lacking the spxB gene encoding pyruvate oxidase, which are deficient in H2O2 production, exhibited reduced cytotoxicity toward Detroit 562 epithelial cells. In addition, enzyme-linked immunosorbent assays revealed that both S. oralis and H2O2 induced interleukin-6 production in Detroit 562 epithelial cells. These results suggest that streptococcal H2O2 is cytotoxic to epithelial cells, and promotes bacterial evasion of the host defense systems in the oral cavity and upper respiratory tracts.
(キーワード): Bacterial Proteins / Cell Death / Cell Line / Epithelial Cells / Humans / Hydrogen Peroxide / Pyruvate Oxidase / Streptococcal Infections / Streptococcus oralis / Streptococcus sanguis
(出版サイトへのリンク): ● Publication site (DOI): 10.1371/journal.pone.0088136
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24498253; ● Search Scopus @ Elsevier (PMID): 24498253; ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0088136

(DOI: 10.1371/journal.pone.0088136, PubMed: 24498253) Nobuo Okahashi, Masanobu Nakata, Tomoko Sumitomo, Yutaka Terao and Shigetada Kawabata :
Hydrogen peroxide produced by oral Streptococci induces macrophage cell death.,
PLoS ONE, Vol.8, No.5, 2013.

(要約): Hydrogen peroxide (H2O2) produced by members of the mitis group of oral streptococci plays important roles in microbial communities such as oral biofilms. Although the cytotoxicity of H2O2 has been widely recognized, the effects of H2O2 produced by oral streptococci on host defense systems remain unknown. In the present study, we investigated the effect of H2O2 produced by Streptococcus oralis on human macrophage cell death. Infection by S. oralis was found to stimulate cell death of a THP-1 human macrophage cell line at multiplicities of infection greater than 100. Catalase, an enzyme that catalyzes the decomposition of H2O2, inhibited the cytotoxic effect of S. oralis. S. oralis deletion mutants lacking the spxB gene, which encodes pyruvate oxidase, and are therefore deficient in H2O2 production, showed reduced cytotoxicity toward THP-1 macrophages. Furthermore, H2O2 alone was capable of inducing cell death. The cytotoxic effect seemed to be independent of inflammatory responses, because H2O2 was not a potent stimulator of tumor necrosis factor-α production in macrophages. These results indicate that streptococcal H2O2 plays a role as a cytotoxin, and is implicated in the cell death of infected human macrophages.
(キーワード): Bacterial Proteins / Catalase / Cell Death / Cell Line / Cytotoxins / Humans / Hydrogen Peroxide / Macrophages / Pyruvate Oxidase / Streptococcus oralis / Tumor Necrosis Factor-alpha
(出版サイトへのリンク): ● Publication site (DOI): 10.1371/journal.pone.0062563
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23658745; ● Search Scopus @ Elsevier (PMID): 23658745; ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0062563

(DOI: 10.1371/journal.pone.0062563, PubMed: 23658745) Mariko Honda-Ogawa, Taiji Ogawa, Yutaka Terao, Tomoko Sumitomo, Masanobu Nakata, Kazunori Ikebe, Yoshinobu Maeda and Shigetada Kawabata :
Cysteine proteinase from Streptococcus pyogenes enables evasion of innate immunity via degradation of complement factors.,
The Journal of Biological Chemistry, Vol.288, No.22, 15854-15864, 2013.

(要約): Streptococcus pyogenes is an important human pathogen that causes invasive diseases such as necrotizing fasciitis, sepsis, and streptococcal toxic shock syndrome. We investigated the function of a major cysteine protease from S. pyogenes that affects the amount of C1-esterase inhibitor (C1-INH) and other complement factors and aimed to elucidate the mechanism involved in occurrence of streptococcal toxic shock syndrome from the aspect of the complement system. First, we revealed that culture supernatant of a given S. pyogenes strain and recombinant SpeB degraded the C1-INH. Then, we determined the N-terminal sequence of the C1-INH fragment degraded by recombinant SpeB. Interestingly, the region containing one of the identified cleavage sites is not present in patients with C1-INH deficiency. Scanning electron microscopy of the speB mutant incubated in human serum showed the abnormal superficial architecture and irregular oval structure. Furthermore, unlike the wild-type strain, that mutant strain showed lower survival capacity than normal as compared with heat-inactivated serum, whereas it had a significantly higher survival rate in serum without the C1-INH than in normal serum. Also, SpeB degraded multiple complement factors and the membrane attack complex. Flow cytometric analyses revealed deposition of C9, one of the components of membrane the attack complex, in greater amounts on the surface of the speB mutant, whereas lower amounts of C9 were bound to the wild-type strain surface. These results suggest that SpeB can interrupt the human complement system via degrading the C1-INH, thus enabling S. pyogenes to evade eradication in a hostile environment.
(キーワード): Bacterial Proteins / Complement C1 Inhibitor Protein / Complement C9 / Complement Membrane Attack Complex / Cysteine Endopeptidases / Exotoxins / Humans / Immune Evasion / Immunity, Innate / Protein Structure, Tertiary / Proteolysis / Streptococcus pyogenes
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M113.469106
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23589297; ● Search Scopus @ Elsevier (PMID): 23589297; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M113.469106

(DOI: 10.1074/jbc.M113.469106, PubMed: 23589297) Tomoko Sumitomo, Masanobu Nakata, Miharu Higashino, Yutaka Terao and Shigetada Kawabata :
Group A streptococcal cysteine protease cleaves epithelial junctions and contributes to bacterial translocation.,
The Journal of Biological Chemistry, Vol.288, No.19, 13317-13324, 2013.

(要約): SpeB-mediated dysfunction of the epithelial barrier may have important implications for not only bacterial invasion but also dissemination of other virulence factors throughout intercellular spaces. Group A Streptococcus (GAS) is an important human pathogen that possesses an ability to translocate across the epithelial barrier. In this study, culture supernatants of tested GAS strains showed proteolytic activity against human occludin and E-cadherin. Utilizing various types of protease inhibitors and amino acid sequence analysis, we identified SpeB (streptococcal pyrogenic exotoxin B) as the proteolytic factor that cleaves E-cadherin in the region neighboring the calcium-binding sites within the extracellular domain. The cleaving activities of culture supernatants from several GAS isolates were correlated with the amount of active SpeB, whereas culture supernatants from an speB mutant showed no such activities. Of note, the wild type strain efficiently translocated across the epithelial monolayer along with cleavage of occludin and E-cadherin, whereas deletion of the speB gene compromised those activities. Moreover, destabilization of the junctional proteins was apparently relieved in cells infected with the speB mutant, as compared with those infected with the wild type. Taken together, our findings indicate that the proteolytic efficacy of SpeB in junctional degradation allows GAS to invade deeper into tissues.
(キーワード): Antigens, CD / Bacterial Proteins / Bacterial Translocation / Caco-2 Cells / Cadherins / Cysteine Endopeptidases / Electric Impedance / Epithelial Cells / Epithelium / Exotoxins / Host-Pathogen Interactions / Humans / Intercellular Junctions / Protein Structure, Tertiary / Proteolysis / Sequence Deletion / Streptococcal Infections / Streptococcus pyogenes
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M113.459875
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23532847; ● Search Scopus @ Elsevier (PMID): 23532847; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M113.459875

(DOI: 10.1074/jbc.M113.459875, PubMed: 23532847) Richard Keiji Kimura, Masanobu Nakata, Tomoko Sumitomo, Bernd Kreikemeyer, Andreas Podbielski, Yutaka Terao and Shigetada Kawabata :
Involvement of T6 pili in biofilm formation by serotype M6 Streptococcus pyogenes.,
Journal of Bacteriology, Vol.194, No.4, 804-812, 2011.

(要約): The group A streptococcus (GAS) Streptococcus pyogenes is known to cause self-limiting purulent infections in humans. The role of GAS pili in host cell adhesion and biofilm formation is likely fundamental in early colonization. Pilus genes are found in the FCT (fibronectin-binding protein, collagen-binding protein, and trypsin-resistant antigen) genomic region, which has been classified into nine subtypes based on the diversity of gene content and nucleotide sequence. Several epidemiological studies have indicated that FCT type 1 strains, including serotype M6, produce large amounts of monospecies biofilm in vitro. We examined the direct involvement of pili in biofilm formation by serotype M6 clinical isolates. In the majority of tested strains, deletion of the tee6 gene encoding pilus shaft protein T6 compromised the ability to form biofilm on an abiotic surface. Deletion of the fctX and srtB genes, which encode pilus ancillary protein and class C pilus-associated sortase, respectively, also decreased biofilm formation by a representative strain. Unexpectedly, these mutant strains showed increased bacterial aggregation compared with that of the wild-type strain. When the entire FCT type 1 pilus region was ectopically expressed in serotype M1 strain SF370, biofilm formation was promoted and autoaggregation was inhibited. These findings indicate that assembled FCT type 1 pili contribute to biofilm formation and also function as attenuators of bacterial aggregation. Taken together, our results show the potential role of FCT type 1 pili in the pathogenesis of GAS infections.
(キーワード): Aminoacyltransferases / Bacterial Adhesion / Bacterial Proteins / Base Sequence / Biofilms / Cysteine Endopeptidases / Fimbriae Proteins / Fimbriae, Bacterial / Humans / Sequence Deletion / Streptococcal Infections / Streptococcus pyogenes
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/JB.06283-11
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22155780; ● Search Scopus @ Elsevier (PMID): 22155780; ● Search Scopus @ Elsevier (DOI): 10.1128/JB.06283-11

(DOI: 10.1128/JB.06283-11, PubMed: 22155780) Tomoko Sumitomo, Masanobu Nakata, Masaya Yamaguchi, Yutaka Terao and Shigetada Kawabata :
S-carboxymethylcysteine inhibits adherence of Streptococcus pneumoniae to human alveolar epithelial cells.,
Journal of Medical Microbiology, Vol.61, No.Pt 1, 101-108, 2011.

(要約): Streptococcus pneumoniae is a major pathogen of respiratory infections that utilizes platelet-activating factor receptor (PAFR) for firm adherence to host cells. The mucolytic agent S-carboxymethylcysteine (S-CMC) has been shown to exert inhibitory effects against infection by several respiratory pathogens including S. pneumoniae in vitro and in vivo. Moreover, clinical studies have implicated the benefits of S-CMC in preventing exacerbation of chronic obstructive pulmonary disease, which is considered to be related to respiratory infections. In this study, to assess whether the potency of S-CMC is attributable to inhibition of pneumococcal adherence to host cells, an alveolar epithelial cell line stimulated with interleukin-1α was used as a model of inflamed epithelial cells. Despite upregulation of PAFR by inflammatory activation, treatment with S-CMC efficiently inhibited pneumococcal adherence to host epithelial cells. In order to gain insight into the inhibitory mechanism, the effects of S-CMC on PAFR expression were also investigated. Following treatment with S-CMC, PAFR expression was reduced at both mRNA and post-transcriptional levels. Interestingly, S-CMC was also effective in inhibiting pneumococcal adherence to cells transfected with PAFR small interfering RNAs. These results indicate S-CMC as a probable inhibitor targeting numerous epithelial receptors that interact with S. pneumoniae.
(キーワード): Alveolar Epithelial Cells / Anti-Infective Agents, Local / Bacterial Adhesion / Carbocysteine / Cell Line, Tumor / Epithelial Cells / Humans / Platelet Membrane Glycoproteins / Pulmonary Alveoli / Receptors, G-Protein-Coupled / Streptococcus pneumoniae
(出版サイトへのリンク): ● Publication site (DOI): 10.1099/jmm.0.033688-0
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21890513; ● Search Scopus @ Elsevier (PMID): 21890513; ● Search Scopus @ Elsevier (DOI): 10.1099/jmm.0.033688-0

(DOI: 10.1099/jmm.0.033688-0, PubMed: 21890513) Masanobu Nakata, Richard Keiji Kimura, Tomoko Sumitomo, Satoshi Wada, Akinari Sugauchi, Eiji Oiki, Miharu Higashino, Bernd Kreikemeyer, Andreas Podbielski, Nobuo Okahashi, Shigeyuki Hamada, Ryutaro Isoda, Yutaka Terao and Shigetada Kawabata :
Assembly mechanism of FCT region type 1 pili in serotype M6 Streptococcus pyogenes.,
The Journal of Biological Chemistry, Vol.286, No.43, 37566-37577, 2011.

(要約): The human pathogen Streptococcus pyogenes produces diverse pili depending on the serotype. We investigated the assembly mechanism of FCT type 1 pili in a serotype M6 strain. The pili were found to be assembled from two precursor proteins, the backbone protein T6 and ancillary protein FctX, and anchored to the cell wall in a manner that requires both a housekeeping sortase enzyme (SrtA) and pilus-associated sortase enzyme (SrtB). SrtB is primarily required for efficient formation of the T6 and FctX complex and subsequent polymerization of T6, whereas proper anchoring of the pili to the cell wall is mainly mediated by SrtA. Because motifs essential for polymerization of pilus backbone proteins in other Gram-positive bacteria are not present in T6, we sought to identify the functional residues involved in this process. Our results showed that T6 encompasses the novel VAKS pilin motif conserved in streptococcal T6 homologues and that the lysine residue (Lys-175) within the motif and cell wall sorting signal of T6 are prerequisites for isopeptide linkage of T6 molecules. Because Lys-175 and the cell wall sorting signal of FctX are indispensable for substantial incorporation of FctX into the T6 pilus shaft, FctX is suggested to be located at the pilus tip, which was also implied by immunogold electron microscopy findings. Thus, the elaborate assembly of FCT type 1 pili is potentially organized by sortase-mediated cross-linking between sorting signals and the amino group of Lys-175 positioned in the VAKS motif of T6, thereby displaying T6 and FctX in a temporospatial manner.
(キーワード): Amino Acid Motifs / Base Sequence / Cell Wall / Fimbriae Proteins / Fimbriae, Bacterial / Humans / Molecular Sequence Data / Protein Multimerization / Streptococcus pyogenes
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M111.239780
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21880740; ● Search Scopus @ Elsevier (PMID): 21880740; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M111.239780

(DOI: 10.1074/jbc.M111.239780, PubMed: 21880740) Nobuo Okahashi, Masanobu Nakata, Yutaka Terao, Ryutaro Isoda, Atsuo Sakurai, Tomoko Sumitomo, Masaya Yamaguchi, K Richard Kimura, Eiji Oiki, Shigetada Kawabata and Takashi Ooshima :
Pili of oral Streptococcus sanguinis bind to salivary amylase and promote the biofilm formation.,
Microbial Pathogenesis, Vol.50, No.3-4, 148-154, 2011.

(要約): Streptococcus sanguinis is a member of oral streptococci and one of the most abundant species found in oral biofilm called dental plaque. Colonization of the oral streptococci on the tooth surface depends on the adhesion of bacteria to salivary components adsorbed to the tooth surface. Recently, we identified unique cell surface long filamentous structures named pili in this species. Herein, we investigated the role of S. sanguinis pili in biofilm formation. We found that pili-deficient mutant, in which the genes encoding the three pilus proteins PilA, PilB and PilC have been deleted, showed an impaired bacterial accumulation on saliva-coated surfaces. Confocal microscopic observations suggested that the mutant was incapable of producing typical three-dimensional layer of biofilm. Ligand blot analysis showed that the ancillary pilus proteins PilB and PilC bound to human whole saliva. Additional analysis demonstrated that PilC bound to multiple salivary components, and one of which was found to be salivary α-amylase. These results indicate that pilus proteins are members of saliva-binding proteins of oral S. sanguinis, and suggest the involvement of pili in its colonization on saliva-coated tooth surfaces and in the human oral cavity.
(キーワード): Amylases / Bacterial Adhesion / Bacterial Proteins / Biofilms / Fimbriae Proteins / Fimbriae, Bacterial / Humans / Mouth / Protein Binding / Saliva / Streptococcal Infections / Streptococcus sanguis
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.micpath.2011.01.005
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21238567; ● Search Scopus @ Elsevier (PMID): 21238567; ● Search Scopus @ Elsevier (DOI): 10.1016/j.micpath.2011.01.005

(DOI: 10.1016/j.micpath.2011.01.005, PubMed: 21238567) Tomoko Sumitomo, Masanobu Nakata, Miharu Higashino, Yingji Jin, Yutaka Terao, Yukako Fujinaga and Shigetada Kawabata :
Streptolysin S contributes to group A streptococcal translocation across an epithelial barrier.,
The Journal of Biological Chemistry, Vol.286, No.4, 2750-2761, 2010.

(要約): Group A Streptococcus pyogenes (GAS) is a human pathogen that causes local suppurative infections and severe invasive diseases. Systemic dissemination of GAS is initiated by bacterial penetration of the epithelial barrier of the pharynx or damaged skin. To gain insight into the mechanism by which GAS penetrates the epithelial barrier, we sought to identify both bacterial and host factors involved in the process. Screening of a transposon mutant library of a clinical GAS isolate recovered from an invasive episode allowed identification of streptolysin S (SLS) as a novel factor that facilitates the translocation of GAS. Of note, the wild type strain efficiently translocated across the epithelial monolayer, accompanied by a decrease in transepithelial electrical resistance and cleavage of transmembrane junctional proteins, including occludin and E-cadherin. Loss of integrity of intercellular junctions was inhibited after infection with a deletion mutant of the sagA gene encoding SLS, as compared with those infected with the wild type strain. Interestingly, following GAS infection, calpain was recruited to the plasma membrane along with E-cadherin. Moreover, bacterial translocation and destabilization of the junctions were partially inhibited by a pharmacological calpain inhibitor or genetic interference with calpain. Our data indicate a potential function of SLS that facilitates GAS invasion into deeper tissues via degradation of epithelial intercellular junctions in concert with the host cysteine protease calpain.
(キーワード): Bacterial Proteins / Caco-2 Cells / Cadherins / Calpain / Humans / Intercellular Junctions / Pharynx / Respiratory Mucosa / Streptococcal Infections / Streptococcus pyogenes / Streptolysins
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M110.171504
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21084306; ● Search Scopus @ Elsevier (PMID): 21084306; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M110.171504

(DOI: 10.1074/jbc.M110.171504, PubMed: 21084306) Nobuo Okahashi, Masanobu Nakata, Atsuo Sakurai, Yutaka Terao, Tomonori Hoshino, Masaya Yamaguchi, Ryutaro Isoda, Tomoko Sumitomo, Kazuhiko Nakano, Shigetada Kawabata and Takashi Ooshima :
Pili of oral Streptococcus sanguinis bind to fibronectin and contribute to cell adhesion.,
Biochemical and Biophysical Research Communications, Vol.391, No.2, 1192-1196, 2009.

(要約): Streptococcus sanguinis is a predominant bacterium in the human oral cavity and occasionally causes infective endocarditis. We identified a unique cell surface polymeric structure named pili in this species and investigated its functions in regard to its potential virulence. Pili of S. sanguinis strain SK36 were shown to be composed of three distinctive pilus proteins (PilA, PilB, and PilC), and a pili-deficient mutant demonstrated reduced bacterial adherence to HeLa and human oral epithelial cells. PilC showed a binding ability to fibronectin, suggesting that pili are involved in colonization by this species. In addition, ATCC10556, a standard S. sanguinis strain, was unable to produce pili due to defective pilus genes, which indicates a diversity of pilus expression among various S. sanguinis strains.
(キーワード): Bacterial Adhesion / Bacterial Proteins / Fibronectins / Fimbriae, Bacterial / Humans / Mouth / Streptococcus sanguis
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2009.12.029
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20004645; ● Search Scopus @ Elsevier (PMID): 20004645; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2009.12.029

(DOI: 10.1016/j.bbrc.2009.12.029, PubMed: 20004645) Akihiro Shirai, Tomoko Sumitomo, Mayuko Kurimoto, Hideaki Maseda and Hiroki Kourai :
The mode of the antifungal activity of gemini-pyridinium salt against yeast,
Biocontrol Science, Vol.14, No.1, 13-20, 2009.

(要約): The gemini quaternary salt (gemini-QUAT) containing two pyridinium residues per molecule, 3,3'-(2,7-dioxaoctane) bis (1-decylpyridinium bromide) (3DOBP-4,10), exerted fungicidal activity against Saccharomyces cerevisiae accompanied by respiration inhibition and the cytoplasmic material leakage of ATP, magnesium, and potassium ions. We previously found that gemini-QUAT exerted bacterioclastic action against Escherichia coli by causing the rapid and abundant leakage of turbid materials from the cells. In addition, the first stage of the bacterioclastic action was the leakage of magnesium ions, outer membrane protein E, ATP, and lipopolysaccharides. Here, we investigated how the gemini-QUAT 3DOBP-4,10 exerts fungicidal action against S. cerevislae. The results showed that that > or = 0.4 microM 3DOBP-4,10 stopped respiration and that > or = 3.0, 1.0 and 1.0 microM caused the leakage of cytoplasmic components ATP, magnesium and potassium ions, respectively. Scanning and transmission electron micrographs showed a preserved cell wall structure, whereas intracellular organelles were destroyed in cells incubated with 3DOBP-4,10. We postulated that 3DOBP-4,10 exerts its fungicidal action against S. cerevisiae not through cell wall destruction and protein leakage, but rather by penetrating the cell wall and disrupting the membranes of organelles.
(キーワード): Antifungal Agents / Microbial Sensitivity Tests / Microscopy, Electron, Scanning / Microscopy, Electron, Transmission / Oxygen / Pyridinium Compounds / Quaternary Ammonium Compounds / Saccharomyces cerevisiae
(出版サイトへのリンク): ● Publication site (DOI): 10.4265/bio.14.13
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19344094; ● Search Scopus @ Elsevier (PMID): 19344094; ● Search Scopus @ Elsevier (DOI): 10.4265/bio.14.13

(DOI: 10.4265/bio.14.13, PubMed: 19344094) Masanobu Nakata, Thomas Köller, Karin Moritz, Deborah Ribardo, Ludwig Jonas, S Kevin McIver, Tomoko Sumitomo, Yutaka Terao, Shigetada Kawabata, Andreas Podbielski and Bernd Kreikemeyer :
Mode of expression and functional characterization of FCT-3 pilus region-encoded proteins in Streptococcus pyogenes serotype M49.,
Infection and Immunity, Vol.77, No.1, 32-44, 2008.

(要約): The human pathogen Streptococcus pyogenes (group A streptococcus [GAS]) pilus components, suggested to play a role in pathogenesis, are encoded in the variable FCT (fibronectin- and collagen-binding T-antigen) region. We investigated the functions of sortase A (SrtA), sortase C2 (SrtC2), and the FctA protein of the most prevalent type 3 FCT region from a serotype M49 strain. Although it is considered a housekeeping sortase, SrtA's activity is involved in pilus formation in addition to its essentiality for GAS extracellular matrix protein binding, host cell adherence/internalization, survival in human blood, and biofilm formation. SrtC2 activity is crucial for pilus formation but dispensable for the other phenotypes tested in vitro. FctA is the major pilus backbone protein, simultaneously acting as the M49 T antigen, and requires SrtC2 and LepA, a signal peptidase I homologue, for monomeric surface expression and polymerization, respectively. Collagen-binding protein Cpa expression supports pilus formation at the pilus base. Immunofluorescence microscopy and fluorescence-activated cell sorting analysis revealed several unexpected expression patterns, as follows: (i) the monomeric pilus protein FctA was found exclusively at the old poles of GAS cells, (ii) FctA protein expression increased with lower temperatures, and (iii) FctA protein expression was restricted to 20 to 50% of a given GAS M49 population, suggesting regulation by a bistability mode. Notably, disruption of pilus assembly by sortase deletion rendered GAS serotype M49 significantly more aggressive in a dermonecrotic mouse infection model, indicating that sortase activity and, consequently, pilus expression allow a subpopulation of this GAS serotype to be less aggressive. Thus, pilus expression may not be a virulence attribute of GAS per se.
(キーワード): Animals / Bacterial Proteins / Blood / Cell Adhesion / Cell Line / Fimbriae, Bacterial / Gene Expression Regulation, Bacterial / Gene Order / Humans / Mice / Microbial Viability / Skin / Skin Diseases, Bacterial / Streptococcal Infections / Streptococcus pyogenes / Virulence / Virulence Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/IAI.00772-08
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18852238; ● Search Scopus @ Elsevier (PMID): 18852238; ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.00772-08

(DOI: 10.1128/IAI.00772-08, PubMed: 18852238) 白井昭博, 住友倫子, 岡村菜穂, 大久保彰洋, 湯浅明彦, 間世田英明, 高麗寛紀 :
銀担持アクリル繊維を含む抗菌紙の魚病原因細菌に対する殺菌特性,
防菌防黴誌, Vol.36, No.9, 579-585, 2008年.

(要約): 銀担持アクリル繊維，ポリエステル，ポロプロピレンの3種混抄紙(izi)の魚病原因細菌に対する殺菌特性を明らかにした．iziは，アユ養殖場から分離された魚病原因細菌に対して強い殺菌力を有していた．また，iziの殺菌力は，一般細菌と魚病原因細菌を含むアユ養殖場のプール水の殺菌に有効であることを示した．
(キーワード): Silver-supported acrylic fiber / 銀担持アクリル繊維 / Bactericidal activity / 殺菌活性 / Fish diseases / 魚病 / Hydroxyl radical disinfection / ヒドロキシラジカル殺菌
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1520009410063770496

(CiNii: 1520009410063770496) Tomoko Sumitomo, Akihiro Shirai, Takuya Maeda, Hideaki Nagamune and Hiroki Kourai :
Construction of a leftover bath water model for microbial testing,
Biocontrol Science, Vol.11, No.3, 107-114, 2006.

(要約): In this study, in order to construct a model of leftover bath water, we analyzed one hundred samples of used bath water samples which were provided by twenty-eight volunteer families. It appeared that the number of detected bacteria from such bath water was correlated closely with the number of bathers. Moreover, the pH, acidity, chemical oxygen demand (COD), ion, protein content of the leftover bath water were measured. The number of bathers had no connection with the pH, acidity, COD, and ion content of the leftover bath water. However, the protein content of the bath water correlated with the number of detected bacteria. Based on these results, the model of leftover bath water was constructed. Achromobacter xylosoxidans, Staphylococcus aureus, Staphylococcus epidermidis, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa were incubated with the model bath water as indices of bath water contamination. The number of incubated viable cells in the model bath water increased with increasing concentrations of casamino acid. Consequently, it was suggested that varying the concentration of casamino acid based on family size or contamination would be necessary in the efficient use of the constructed model of leftover bath water for microbial testing.
(キーワード): Baths / Colony Count, Microbial / Conservation of Natural Resources / Escherichia coli / Humans / Hydrogen-Ion Concentration / Klebsiella pneumoniae / Laundering / Microbiological Techniques / Models, Biological / Pseudomonas aeruginosa / Staphylococcus aureus / Staphylococcus epidermidis / Water / Water Microbiology
(出版サイトへのリンク): ● Publication site (DOI): 10.4265/bio.11.107
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17017128; ● Search Scopus @ Elsevier (PMID): 17017128; ● Search Scopus @ Elsevier (DOI): 10.4265/bio.11.107

(DOI: 10.4265/bio.11.107, PubMed: 17017128) Tomoko Sumitomo, Hideaki Nagamune, Takuya Maeda and Hiroki Kourai :
Correlation between the Bacterioclastic Action of a Bis-quaternary Ammonium Compound and Outer Membrane Proteins,
Biocontrol Science, Vol.11, No.3, 115-124, 2006.

(要約): Bis-quaternary ammonium compounds (bis-QACs) have the ability to cause a rapid and abundant leakage of the turbid materials from cells, and such a bacterioclastic ability leads to a potent bactericidal activity. In order to clarify the detailed mechanism of the bactericidal action of bis-QACs, the correlation between the bacterioclastic action of 4,4'-(1,6-hexamethylenedithio)bis(1-octylpyridinium bromide) (4DTBP-6,8) and the leakage of outer membrane pore protein E (OmpE) was investigated. Using the antiserum against a fusion protein consisting of GST and the OmpE protein of Escherichia coli encoded by the ompE gene, it was seen that the leakage of OmpE from E. coli cells was caused by treatment with low concentrations (much lower than the critical vesiculation concentration) of 4DTBP-6,8. Furthermore, it was confirmed that 4DTBP-6,8 caused an increase in the turbidity of the cell suspension of Klebsiella pneumoniae, Salmonella typhimurium and Serratia marcescences, and led to the leakage of several proteins which have a high percentage of homology with OmpE of E. coll. By immunoelectron microscopy investigation, it was revealed that the vesiculation from E. coli treated with 4DTBP-6,8 contains OmpE. In addition, the bacteriolytic action of 4DTBP-6,8 was investigated. The results suggested that the lysis of cells by bis-QACs was not an enzymatic action such as that by autolysin but a physical bacterioclastic action. Judging from these results, it is suggested that the leakage of OmpE is one of the major bacterioclastic actions of bis-QACs, and deals the bacterial cells a fatal blow.
(キーワード): Anti-Bacterial Agents / Bacterial Outer Membrane Proteins / Base Sequence / DNA, Bacterial / Disinfectants / Escherichia coli / Escherichia coli Proteins / Microscopy, Immunoelectron / Quaternary Ammonium Compounds / Recombinant Fusion Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.4265/bio.11.115
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17017129; ● CiNii @ 国立情報学研究所 (CRID): 1390282679441112960; ● Search Scopus @ Elsevier (PMID): 17017129; ● Search Scopus @ Elsevier (DOI): 10.4265/bio.11.115

(DOI: 10.4265/bio.11.115, PubMed: 17017129, CiNii: 1390282679441112960) Akihiro Shirai, Tomoko Sumitomo, Munehiro Yoshida, Tomoyo Kaimura, Hideaki Nagamune, Takuya Maeda and Hiroki Kourai :
Synthesis and biological properties of gemini quaternary ammonium compounds,5,5'-[2,2'-(α,ω-polymethylnedicarbonyldioxy)diethyl]bis(3-alkyl-4-methylthiazolium iodide) and 5,5'- [2,2'-(ρ-phenylenedicarbonyldioxy)diethyl] bis(3-alkyl-4-methylthiazolium bromide),
Chemical & Pharmaceutical Bulletin, Vol.54, No.5, 639-645, 2006.

(要約): We synthesized gemini quaternary ammonium compounds (gemini QACs) having two thiazolium moieties in a molecule, 5,5'-[2,2'-(alpha,omega-polymethylnedicarbonyldioxy)diethyl]bis(3-alkyl-4-methylthiazolium iodide) (5DEBT-m,n), on which the carbon number of the methylene chain linking the two thiazoles (m) is 2, 6 or 8 and that of the alkyl group (n) is 8, 10, 12, 14 or 16. 5,5'-[2,2'-(p-Phenylenedicarbonyldioxy)diethyl]bis(3-alkyl-4-methylthiazolium bromide) (5DEBT-P,n) was then synthesized, which is composed of a p-phenylene as the methylene spacer. For five gemini QAC series, in addition to the previously described 5DEBT-4,n to the four new compound series, their antimicrobial activities were determined. 5DEBT-m,10 and -P,10 exhibited a wide and strong bacteriostatic activity against gram-negative and -positive bacteria, fungi and then yeast in comparison with N-tetradecyl-5-(2-hydroxyethyl)-4-methylthiazolium iodide as a mono-QAC. The bactericidal activity of the 5DEBT series against Escherichia coli IFO 12713 and Staphylococcus aureus IFO 12732 was investigated on the basis of the effects of their alkyl chain length and their molecular hydrophobicity. It was found that the effect of theses factors on their activity significantly changes by the difference between the gram-negative and -positive bacteria. Although against the gram-negative bacterium, the change in the activity due to extension of the alkyl group for each compound affected the kind of methylene spacer, against the gram-positive bacterium, it was almost equal in spite of the methylene spacer. This result could be responsible for the bactericidal mechanism of the gemini QACs being influenced by the diversity of the steric structure participating in the methylene chain length and by the bacterium cell surface hydrophobicity.
(キーワード): Alkylation / Anti-Bacterial Agents / Anti-Infective Agents / Antifungal Agents / Chemistry, Physical / Chromatography, Thin Layer / Escherichia coli / Fungi / Magnetic Resonance Spectroscopy / Microbial Sensitivity Tests / Physicochemical Phenomena / Quaternary Ammonium Compounds / Staphylococcus aureus / Structure-Activity Relationship / Thiazoles / Yeasts
(出版サイトへのリンク): ● Publication site (DOI): 10.1248/cpb.54.639
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16651758; ● Search Scopus @ Elsevier (PMID): 16651758; ● Search Scopus @ Elsevier (DOI): 10.1248/cpb.54.639

(DOI: 10.1248/cpb.54.639, PubMed: 16651758) 住友倫子, 幸坂葵, 中秀雄, 前田拓也, 高麗寛紀 :
繊維製品の抗真菌性試験,
防菌防黴誌, Vol.34, No.3, 141-147, 2006年.

MISC

研究者総覧に該当データはありませんでした。

総説・解説

Tomoko Sumitomo and Shigetada Kawabata :
Respiratory tract barrier dysfunction in viral-bacterial co-infection cases,
Japanese Dental Science Review, Vol.60, 44-52, Dec. 2024.

(徳島大学機関リポジトリ): ● Metadata: 119256
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.jdsr.2023.12.006
(文献検索サイトへのリンク): ● Search Scopus @ Elsevier (DOI): 10.1016/j.jdsr.2023.12.006

(徳島大学機関リポジトリ: 119256, DOI: 10.1016/j.jdsr.2023.12.006) 住友倫子, 川端重忠 :
インフルエンザに合併する細菌性肺炎の重要性,
歯界月報, Vol.848, 1-6, 2022年.

(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1010294643572774016

(CiNii: 1010294643572774016) 住友倫子 :
化膿レンサ球菌の上皮バリア突破機構,
日本細菌学雑誌, Vol.72, No.3, 213-218, 2017年.

(要約): Streptococcus pyogenes is a β-hemolytic organism responsible for a wide variety of human diseases that commonly occur as self-limiting purulent diseases of the pharynx and skin. Although the occurrence of invasive infections by S. pyogenes is rare, mortality rates remain high even with progressive medical therapy. As a prerequisite for causing the severe invasive disease, S. pyogenes must invade underlying sterile tissues by translocating across the epithelial barrier. In this study, streptolysin S and SpeB were identified as the novel factors that facilitate bacterial translocation via degradation of intercellular junctions. Furthermore, we found that S. pyogenes exploits host plasminogen for acceleration of bacterial invasion into deeper tissues via tricellular tight junctions. Here, I would like to show our study on bacterial translocation across the epithelial barrier through paracellular route.
(キーワード): Bacterial Proteins / Bacterial Translocation / Epithelial Cells / Epithelium / Exotoxins / Humans / Intercellular Junctions / Plasminogen / Streptococcal Infections / Streptococcus pyogenes / Streptolysins / Tight Junctions
(出版サイトへのリンク): ● Publication site (DOI): 10.3412/jsb.72.213
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28845032; ● Search Scopus @ Elsevier (PMID): 28845032; ● Search Scopus @ Elsevier (DOI): 10.3412/jsb.72.213

(DOI: 10.3412/jsb.72.213, PubMed: 28845032) 住友倫子 :
細胞間隙経路を介した化膿レンサ球菌の上皮バリア突破機構,
大阪大学歯学雑誌, Vol.60, No.1, 15-19, 2015年. 住友倫子, 川端重忠 :
劇症型溶血性レンサ球菌感染症の発症に寄与する細菌因子．特集「いわゆるヒト喰いバクテリアと劇症型感染症」,
化学療法の領域, Vol.29, No.7, 1430-1437, 2013年. 住友倫子, 川端重忠 :
レンサ球菌の新たな理解に向けて. 特集「病原体の感染戦略における新たな知見」,
化学療法の領域, Vol.23, No.11, 1741-1747, 2007年. 前田拓也, 住友倫子, 高麗寛紀 :
食品衛生と界面活性剤4, --- 界面活性剤の殺菌·抗菌作用 ---,
防菌防黴誌, Vol.33, No.10, 550-560, 2005年10月.

講演・発表

Yamaguchi Masaya, Higashi Kotaro, Takebe Katsuki, Nakata Masanobu, Tomoko Sumitomo and Kawabata Shigetada :
Structural analysis of inactive hyaluronidase of Streptococcus pyogenes,
The 16th Japan-Korea International Symposium on Microbiology, Aug. 2024. Higashi Kotaro, Yamaguchi Masaya, Takebe Katsuki, Nakata Masanobu, Tomoko Sumitomo, Suzuki Mamoru, Nizet Victor and Kawabata Shigetada :
Hyaluronidase in Streptococcus pyogenes analysis based on structural biology and molecular phylogenetics,
Society for Glycobiology 2023 Annual meeting, Nov. 2023. Raras Ajeng Enggardipta, Minato Akizuki, Tomoko Sumitomo, Kazumitsu Sekine, Kenichi Hamada and Hiromichi Yumoto :
Comparison of Chitosan with Different Molecular Weights as Possible Antibiofilm Materials Against Enterococcus faecalis Biofilms,
The 22nd Scientific Congress of the Asian Pacific Endodontic Confederation (APEC) 2023, Aug. 2023. Tomoko Sumitomo and Hiroki Kourai :
Bacterioclastic Action of a Gemini-Quaternary Ammonium Compound,
Membrane Stress Biotechnology Symposium, Sep. 2006. Okamura Keekushan, Iwata Mana, Kato Kohsuke, Tomoko Sumitomo and Kawaguchi Atsushi :
Activation mechanism of commensal Streptococcus pneumoniae by macrophage differentiation upon influenza A virus infection,
第70回日本ウイルス学会学術集会, Sep. 2023. 中村勇紀, 岩田真奈, 加藤広介, 住友倫子, 川口敦史 :
上気道常在細菌を起因としたA型インフルエンザウイルス感染による二次性細菌性肺炎マウスモデルの開発,
第70回日本ウイルス学会学術集会, 2023年9月. 大野誠之, 山口雅也, 元岡大祐, 広瀬雄二郎, 東孝太郎, 秋山徹, 住友倫子, 池辺忠義, 山口貴弘, 河原隆二, 奥野ルミ, 大塚仁, 松本裕子, 賀澤優, 川端重忠 :
オミクス解析を用いたemm89型化膿レンサ球菌侵襲性感染症の発症に関与する,
第8回口腔微生物研究会, 2023年9月. 住友倫子, 川端重忠 :
新規感染制御法の確立に向けた細菌性肺炎の重症化機構の解明,
第65回歯科基礎医学会学術大会, 2023年9月. 中田匡宣, 窪田星子, 広瀬雄二郎, 山口雅也, 住友倫子, 川端重忠 :
化膿レンサ球菌のRNase Yによる線毛産生量の調節,
第65回歯科基礎医学会学術大会, 2023年9月. 松本愛理, 大貝悠一, 住友倫子, 中田匡宣 :
ミティス群レンサ球菌が産生する細胞外小胞の作用特性の解明,
第65回歯科基礎医学会学術大会, 2023年9月. 武部克希, 鈴木守, 東孝太郎, 山口雅也, 住友倫子, 川端重忠, 中田匡宣 :
Streptococcus sanguinis が産生する線毛タンパク質のX線結晶構造解析,
第65回歯科基礎医学会学術大会, 2023年9月. 松本愛理, 大貝悠一, 田端厚之, 住友倫子, 中田匡宣 :
ミティス群レンサ球菌における細胞外小胞の産生とその作用特性,
第75回九州微生物研究フォーラム2023, 2023年9月. 大野誠之, 山口雅也, 元岡大祐, 広瀬雄二郎, 東孝太郎, 秋山徹, 住友倫子, 池辺忠義, 山口貴弘, 河原隆二, 奥野ルミ, 大塚仁, 松本裕子, 賀澤優, 中西典子, 川端重忠 :
日本および世界のemm89型化膿レンサ球菌侵襲性感染症に関与する遺伝因子の比較,
第53回レンサ球菌研究会, 2023年7月. 大野誠之, 山口雅也, 元岡大祐, 広瀬雄二郎, 東孝太郎, 秋山徹, 住友倫子, 池辺忠義, 奥野ルミ, 川端重忠 :
侵襲性に関与するemm89型化膿レンサ球菌の因子の探索と分子生物学的解析,
第96回日本細菌学会総会, 2023年3月. 住友倫子 :
インフルエンザに合併する細菌性肺炎の重症化分子機構,
第2回日本医学会連合「Rising Star」リトリート, 2023年3月. 上田昭子, 栗本麻友子, 住友倫子, 白井昭博, 間世田英明, 高麗寛紀 :
酵母に対するジェミニ型第四アンモニウム塩系薬剤の殺菌機構,
第119回徳島生物学会, 2007年12月. 森下裕生, 室巻良彦, 住友倫子, 白井昭博, 間世田英明, 高麗寛紀 :
ジェミニ型第四アンモニウム塩系薬剤の毒性と化学構造の定量的構造活性相関解析,
日本防菌防黴学会第34回年次大会, 2007年8月. 岡村菜穂, 住友倫子, 大久保彰洋, 湯浅明彦, 白井昭博, 間世田英明, 高麗寛紀 :
魚病細菌に対する光触媒抗菌紙の殺菌特性,
日本防菌防黴学会第34回年次大会, 2007年8月. 白井昭博, 栗本麻友子, 住友倫子, 間世田英明, 高麗寛紀 :
酵母に対するジェミニ型ピリジニウム塩系薬剤の殺菌機構,
日本防菌防黴学会第34回年次大会, 2007年8月. 間世田英明, 小中瑠実, 長宗秀明, 住友倫子, 前田拓也, 高麗寛紀 :
Serratia marcescens の消毒剤および抗生物質に対する耐性機構の解明,
日本細菌学会, 2007年3月. 古小路夏美, 住友倫子, 間世田英明, 前田拓也, 高麗寛紀 :
多剤交叉耐性Achromobacter sp.の耐性化機構の解明,
日本防菌防黴学会2006年度若手の会, 2006年10月. 北浦真希, 住友倫子, 前田拓也, 間世田英明, 高麗寛紀 :
セラチアに対するジェミニ型第四アンモニウム塩系薬剤の殺菌機構の解明,
日本防菌防黴学会2006年度若手の会, 2006年10月. 上田昭子, 栗本麻友子, 住友倫子, 前田拓也, 間世田英明, 高麗寛紀 :
酵母に対するジェミニ型第四アンモニウム塩系薬剤の殺菌機構,
日本防菌防黴学会2006年度若手の会, 2006年10月. 岡村菜穂, 住友倫子, 前田拓也, 間世田英明, 高麗寛紀 :
gemini型第四アンモニウム塩の枯草菌(Bacillus subtilis)に対する殺菌機構の解明,
日本防菌防黴学会2006年度若手の会, 2006年10月. 渡辺裕子, 住友倫子, 前田拓也, 長宗秀明, 高麗寛紀 :
セラチアの殺菌消毒剤耐性化機構,
日本防菌防黴学会, 2005年11月. 数藤萌, 岡本好子, 住友倫子, 前田拓也, 高麗寛紀 :
MRSAに対するGemini型第四アンモニウム塩の殺菌機構,
日本防菌防黴学会, 2005年11月. 福居麻弓, 射本康夫, 才所未来, 辻陽平, 山本ゆかり, 住友倫子, 前田拓也, 高麗寛紀 :
Gemini型第四アンモニウム塩の抗菌特性,
日本防菌防黴学会, 2005年11月. 住友倫子, 白井昭博, 長宗秀明, 前田拓也, 高麗寛紀 :
ビス型第四アンモニウム塩系薬剤の殺菌メカニズムの解明,
日本防菌防黴学会第32回年次大会, 2005年5月. 住友倫子, 白井昭博, 藪原忠男, 吉成安純, 唐木真理, 渡辺裕子, 浅田舞子, 栗本麻友子, 野々宮正晃, 浜川智江, 林正道, 三上勝弘, 高麗寛紀 :
微生物試験用モデル残り湯の構築,
日本防菌防黴学会第32回年次大会, 2005年5月. 住友倫子, 白井昭博, 藪原忠男, 吉成安純, 唐木真理, 渡辺裕子, 浅田舞子, 栗本麻友子, 野々宮正晃, 浜川智江, 林正道, 三上勝弘, 高麗寛紀 :
風呂残り湯の微生物学的及び化学的解析,
日本防菌防黴学会第32回年次大会, 2005年5月. 住友倫子, 白井昭博, 前田拓也, 長宗秀明, 高麗寛紀 :
ビス型第四アンモニウム塩系殺菌剤の殺菌メカニズムの解明,
日本防菌防黴学会 2004年度若手の会, 2004年10月. 山口文子, 住友倫子, 前田拓也, 長宗秀明, 高麗寛紀 :
ビス型第四級アンモニウム塩系薬剤の殺菌メカニズム,
日本防菌防黴学会第31回年次大会, Vol.IIDp-10, 2004年5月. 住友倫子, 長宗秀明, 前田拓也, 高麗寛紀 :
ビス型第四級アンモニウム塩系薬剤の細胞破壊作用とOmpEの関連性,
日本防菌防黴学会第31回年次大会, Vol.IIDp-8, 2004年5月. 住友倫子, 高麗寛紀, 山仲浩二, 曽田勇作, 青木美保 :
空気殺菌装置の開発と殺菌評価,
日本防菌防黴学会第30回年次大会, 2003年5月.

研究会・報告書: 大野誠之, 山口雅也, 元岡大祐, 広瀬雄二郎, 東孝太郎, 秋山徹, 住友倫子, 池辺忠義, 山口貴弘, 河原隆二, 奥野ルミ, 大塚仁, 松本裕子, 賀澤優, 中西典子, 川端重忠 :
日本および世界のemm89型化膿レンサ球菌侵襲性感染症に関与する遺伝因子の比較,
第53回レンサ球菌研究会, 2023年7月.

特許: 高麗寛紀, 住友倫子 : 抗ウイルス剤, 特願2007-053943 (2007年3月), 特開2008-214268 (2008年9月), .
作品: 研究者総覧に該当データはありませんでした。
補助金・競争的資金: BacPROTACsを活用した歯周病原性バイオフィルム制御技術の創生 (研究課題/領域番号: 24K22190 )
肺炎球菌の細胞壁分解能が病態形成と薬剤耐性獲得に果たす役割の解明 (研究課題/領域番号: 23K27764 )
細菌の耐性化機構を回避するファージ療法の創出 (研究課題/領域番号: 22K19618 )
高齢者気道組織を再現する動物モデルを用いた肺炎発症機構の解明と診断法への応用 (研究課題/領域番号: 23K24559 )
レンサ球菌のニッチ拡大機構の解明と新規感染制御法の探索 (研究課題/領域番号: 23K24520 )
一細胞解析による肺炎球菌感染時の宿主転写応答の解明 (研究課題/領域番号: 20K21675 )
細菌における新規翻訳制御機構の探索 (研究課題/領域番号: 19K22715 )
分子進化情報を活用した耐性化の可能性が低い新たな感染制御法の確立 (研究課題/領域番号: 19K22710 )
病原性レンサ球菌が病態を誘導する分子機構の解明と新規制御法の探索 (研究課題/領域番号: 19H03825 )
細菌性髄膜炎の発症につながる新規細菌伝播経路と感染制御法の探索 (研究課題/領域番号: 18K19643 )
菌体表層に存在する線維状タンパク質重合体の会合と抗原性がもたらす病原性の探索 (研究課題/領域番号: 17K19751 )
トリセルラージャンクションを標的とする病原性レンサ球菌の組織侵入機構の解析 (研究課題/領域番号: 17K11610 )
レンサ球菌のニッチ拡大に伴う宿主-菌体相互作用の解析 (研究課題/領域番号: 17H04369 )
肺炎球菌のアルギニン代謝産物による免疫回避機構の解明 (研究課題/領域番号: 16K15787 )
東南アジア諸国における肺炎球菌の疫学解析と新規病原性の探索 (研究課題/領域番号: 16H05847 )
菌血症の発症および全身伝播に関与するレンサ球菌分子群の探索 (研究課題/領域番号: 15H05012 )
赤色色素オルニチンラムノリピドによる口腔常在細菌のニッチ拡大機構の解析 (研究課題/領域番号: 26670800 )
細胞間隙経路を介した病原性レンサ球菌の組織侵入機構の解析 (研究課題/領域番号: 26462780 )
レンサ球菌が産生する線毛の付着機能と発現機構の解析 (研究課題/領域番号: 26462779 )
Ａ群レンサ球菌による上皮バリア破壊機構の解析 (研究課題/領域番号: 24791961 )
ＤＮＡオリガミを用いた新規免疫アジュバントの開発 (研究課題/領域番号: 24659836 )
シクロデキストリン依存的な口腔細菌の全身伝播機構の解析 (研究課題/領域番号: 24659812 )
補体制御因子を不活化し侵襲性感染症を誘発させる細菌分子の探索 (研究課題/領域番号: 24390410 )
Ａ群レンサ球菌ｎｃＲＮＡによる病原性調節機構の解析 (研究課題/領域番号: 23592700 )
細胞間隙経路を介したA群レンサ球菌の上皮バリア突破機構の解析 (研究課題/領域番号: 20791336 )
ヒト病原性レンサ球菌が産生する付着・定着因子群の機能解析 (研究課題/領域番号: 20390465 )
A群レンサ球菌のフィブロネクチン結合タンパクの感染防御抗原としての可能性 (研究課題/領域番号: 18390489 )
研究者番号（50423421）による検索

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2024年12月23日更新

専門分野・研究分野: 細菌学 (Bacteriology)
口腔細菌学 (Oral Microbiology)
所属学会・所属協会: 日本細菌学会
歯科基礎医学会
委員歴・役員歴: 日本細菌学会 (理事 [2024年1月〜2026年12月])
受賞: 2005年5月, 平成 16 年度日本防菌防黴学会論文賞 (日本防菌防黴学会)
2014年8月, 平成 26 年度歯科基礎医学会学会奨励賞 (歯科基礎医学会)
2017年3月, 平成 28 年度日本細菌学会黒屋奨学賞 (日本細菌学会)
活動: 日本細菌学会 (理事 [2024年1月〜2026年12月])

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2024年12月22日更新

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Ｊグローバル

Jグローバル最終確認日: 2024/12/21 01:18
氏名（漢字）: 住友倫子
氏名（フリガナ）: スミトモトモコ
氏名（英字）: Sumitomo Tomoko
所属機関: 徳島大学教授

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researchmap最終確認日: 2024/12/22 01:14
氏名（漢字）: 住友倫子
氏名（フリガナ）: スミトモトモコ
氏名（英字）: Sumitomo Tomoko
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登録日時: 2018/10/3 13:15
更新日時: 2024/11/11 13:03
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所属ID: 0344000000
所属: 徳島大学
部署: 大学院医歯薬学研究部
職名: 教授
学位: 博士 (工学)
学位授与機関: 徳島大学
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2024年12月21日更新

研究者番号: 50423421

所属（現在）: 2024/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学域), 教授

所属（過去の研究課題 情報に基づく）*注記: 2022/4/1 – 2024/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学域), 教授
2022/4/1 : 大阪大学, 大学院歯学研究科, 講師
2017/4/1 – 2021/4/1 : 大阪大学, 歯学研究科, 講師
2016/4/1 : 大阪大学, 歯学研究科, 助教
2013/4/1 – 2015/4/1 : 大阪大学, 大学院歯学研究科, 助教
2011/4/1 – 2015/4/1 : 大阪大学, 歯学研究科(研究院), 助教
2012/4/1 – 2013/4/1 : 大阪大学, 歯学研究科, 助教
2007/4/1 – 2010/4/1 : 大阪大学, 大学院・歯学研究科, 助教

審査区分/研究分野

研究代表者

生物系 / 医歯薬学 / 歯学 / 形態系基礎歯科学
小区分57080:社会系歯学関連
中区分57:口腔科学およびその関連分野

研究代表者以外

生物系 / 医歯薬学 / 歯学 / 形態系基礎歯科学
生物系 / 医歯薬学 / 歯学 / 病態科学系歯学・歯科放射線学
口腔科学およびその関連分野
中区分57:口腔科学およびその関連分野
小区分57020:病態系口腔科学関連

キーワード

研究代表者

レンサ球菌 / 病原因子 / 組織侵入 / 細胞間隙 / 上皮バリア / 細菌性肺炎 / インフルエンザ / 肺炎 / 高齢者気道組織 / 歯周病原細菌 / Fusobacterium nucleatum / バイオフィルム

研究代表者以外

レンサ球菌 / 線毛 / 付着因子 / 定着因子 / 組織指向性 / A群レンサ球菌 / ncRNA / 細菌 / non-coding RNA / 補体 / 免疫回避 / 感染症 / 免疫 / 補体制御因子 / NETs / 口腔細菌 / シクロデキストリン / 上皮バリア / 口腔常在細菌 / アジュバント / DNAオリガミ / ワクチン / 化膿レンサ球菌 / 細菌由来色素 / Streptococcus pyogenes / フィプロネクチン結合タンパク / FbaA / FbaB / 表層タンパク / 感染防御抗原 / フィブロネクチン結合タンパク / 菌体表層タンパク / fibronectin-binding protein / group A streptococci / vaccine / cell-associated protein / potective antigen / 菌血症 / 病原性レンサ球菌 / 肺炎球菌 / 口腔レンサ球菌 / 分子疫学 / ミャンマー / タイ / 薬剤耐性 / アルギニン / 微生物 / 細菌性髄膜炎 / 血液脳関門 / 分子進化 / 低分子阻害剤 / ゲノムワイド関連解析 / BgaA / ゲノム解析 / 分子進化解析 / 翻訳効率 / エンドリボヌクレアーゼ / mRNA / シングルセル解析 / 肺感染 / 肺胞洗浄液（BALF） / 一細胞解析 / RNA-seq / ATAC-seq / インフルエンザ / A型インフルエンザウイルス / 病原レンサ球菌 / ファージ療法 / 耐性化 / 抗CRISPR分子 / 耐性化回避 / ニッチ / 病原性発揮機構 / 病態形成機構 / 細胞外小胞 / 自己融解 / 細菌シングルセル解析 / 高速原子間力顕微鏡

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住友 倫子

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住友倫子