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Structure of polymerized type V pilin reveals assembly mechanism involving protease-mediated strand exchange
https://oist.repo.nii.ac.jp/records/2554
https://oist.repo.nii.ac.jp/records/2554da875ef5-0285-4b63-a4c9-566e5f80450c
名前 / ファイル | ライセンス | アクション |
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NMICROBIOL-19082155B_final_submission (3.7 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2022-02-15 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Structure of polymerized type V pilin reveals assembly mechanism involving protease-mediated strand exchange | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者(英) |
Shibata, Satoshi
× Shibata, Satoshi× Shoji, Mikio× Okada, Kodai× Matsunami, Hideyuki× Matthews, Melissa M.× Imada, Katsumi× Nakayama, Koji× Wolf, Matthias |
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書誌情報 |
en : Nature Microbiology 巻 5, 号 6, p. 830-837, 発行日 2020-04-13 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Bacterial adhesion is a general strategy for host–microbe and microbe–microbe interactions. Adhesive pili are essential for colonization, biofilm formation, virulence and pathogenesis of many environmental and pathogenic bacteria1,2. Members of the class Bacteroidia have unique type V pili, assembled by protease-mediated polymerization3. Porphyromonas gingivalis is the main contributor to periodontal disease and its type V pili are a key factor for its virulence4. However, the structure of the polymerized pilus and its assembly mechanism are unknown. Here we show structures of polymerized and monomeric states of FimA stalk pilin from P. gingivalis, determined by cryo-electron microscopy and crystallography. The atomic model of assembled FimA shows that the C-terminal strand of a donor subunit is inserted into a groove in the β-sheet of an acceptor subunit after N-terminal cleavage by the protease RgpB. The C terminus of the donor strand is essential for polymerization. We propose that type V pili assemble via a sequential polar assembly mechanism at the cell surface, involving protease-mediated strand exchange, employed by various Gram-negative species belonging to the class Bacteroidia. Our results reveal functional surfaces related to pathogenic properties of polymerized FimA. These insights may facilitate development of antibacterial drugs. | |||||
出版者 | ||||||
出版者 | Nature Portfolio | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 2058-5276 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/32284566 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.1038/s41564-020-0705-1 | |||||
権利 | ||||||
権利情報 | © 2020 The Author(s). | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.nature.com/articles/s41564-020-0705-1 | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa |