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N-Linked Glycosylation on Anthrax Toxin Receptor 1 Is Essential for Seneca Valley Virus Infection
https://oist.repo.nii.ac.jp/records/2130
https://oist.repo.nii.ac.jp/records/2130c6483715-feed-4e9d-9ad0-f387602900e9
名前 / ファイル | ライセンス | アクション |
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Jayawardena-2021-N-Linked Glycosylation on Ant (7.7 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 | 2021-05-24 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | N-Linked Glycosylation on Anthrax Toxin Receptor 1 Is Essential for Seneca Valley Virus Infection | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | virus receptor interaction | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | receptor glycosylation | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | picornavirus | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | icosahedral capsid | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | cryo-electron microscopy | |||||
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) |
Jayawardena, Nadishka
× Jayawardena, Nadishka× Miles, Linde A.× Burga, Laura N.× Rudin, Charles× Wolf, Matthias× Poirier, John T.× Bostina, Mihnea |
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書誌情報 |
en : Viruses 巻 13, 号 5, p. 769, 発行日 2021-04-28 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Seneca Valley virus (SVV) is a picornavirus with potency in selectively infecting and lysing cancerous cells. The cellular receptor for SVV mediating the selective tropism for tumors is anthrax toxin receptor 1 (ANTXR1), a type I transmembrane protein expressed in tumors. Similar to other mammalian receptors, ANTXR1 has been shown to harbor N-linked glycosylation sites in its extracellular vWA domain. However, the exact role of ANTXR1 glycosylation on SVV attachment and cellular entry was unknown. Here we show that N-linked glycosylation in the ANTXR1 vWA domain is necessary for SVV attachment and entry. In our study, tandem mass spectrometry analysis of recombinant ANTXR1-Fc revealed the presence of complex glycans at N166, N184 in the vWA domain, and N81 in the Fc domain. Symmetry-expanded cryo-EM reconstruction of SVV-ANTXR1-Fc further validated the presence of N166 and N184 in the vWA domain. Cell blocking, co-immunoprecipitation, and plaque formation assays confirmed that deglycosylation of ANTXR1 prevents SVV attachment and subsequent entry. Overall, our results identified N-glycosylation in ANTXR1 as a necessary post-translational modification for establishing stable interactions with SVV. We anticipate our findings will aid in selecting patients for future cancer therapeutics, where screening for both ANTXR1 and its glycosylation could lead to an improved outcome from SVV therapy. | |||||
出版者 | ||||||
出版者 | MDPI | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1999-4915 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/33924774 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.3390/v13050769 | |||||
権利 | ||||||
権利情報 | © 2021 The Author(s). | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.mdpi.com/1999-4915/13/5/769 | |||||
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 |