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Structures of distant diphtheria toxin homologs reveal functional determinants of an evolutionarily conserved toxin scaffold
https://oist.repo.nii.ac.jp/records/2638
https://oist.repo.nii.ac.jp/records/2638fc1a6316-ccc3-4898-aff6-e35b21a2bc32
名前 / ファイル | ライセンス | アクション |
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Sugiman-Marango-2022-Structures of distant dip (2.5 MB)
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Creative Commons Attribution 4.0 International (https://creativecommons.org/licenses/by/4.0/)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2022-05-17 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Structures of distant diphtheria toxin homologs reveal functional determinants of an evolutionarily conserved toxin scaffold | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | molecular evolution | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Pathogens | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Transferases | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | X-ray crystallography | |||||
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) |
Sugiman-Marangos, Seiji N.
× Sugiman-Marangos, Seiji N.× Gill, Shivneet K.× Mansfield, Michael J.× Orrell, Kathleen E.× Doxey, Andrew C.× Melnyk, Roman A. |
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書誌情報 |
en : Communications Biology 巻 5, 号 1, p. 375, 発行日 2022-04-19 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Diphtheria toxin (DT) is the archetype for bacterial exotoxins implicated in human diseases and has played a central role in defining the field of toxinology since its discovery in 1888. Despite being one of the most extensively characterized bacterial toxins, the origins and evolutionary adaptation of DT to human hosts remain unknown. Here, we determined the first high-resolution structures of DT homologs outside of the Corynebacterium genus. DT homologs from Streptomyces albireticuli (17% identity to DT) and Seinonella peptonophila (20% identity to DT), despite showing no toxicity toward human cells, display significant structural similarities to DT sharing both the overall Y-shaped architecture of DT as well as the individual folds of each domain. Through a systematic investigation of individual domains, we show that the functional determinants of host range extend beyond an inability to bind cellular receptors; major differences in pH-induced pore-formation and cytosolic release further dictate the delivery of toxic catalytic moieties into cells, thus providing multiple mechanisms for a conserved structural fold to adapt to different hosts. Our work provides structural insights into the expanding DT family of toxins, and highlights key transitions required for host adaptation. | |||||
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 | 2399-3642 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/35440624 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.1038/s42003-022-03333-9 | |||||
権利 | ||||||
権利情報 | © 2022 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/s42003-022-03333-9#citeas | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |