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  1. B300 農学部/生命農学研究科
  2. B300a 雑誌掲載論文
  3. 学術雑誌

Molecular basis of N-glycan recognition by pradimicin a and its potential as a SARS-CoV-2 entry inhibitor

http://hdl.handle.net/2237/0002011644
http://hdl.handle.net/2237/0002011644
607d065c-0a4f-43ac-bec3-cc410bcf91db
名前 / ファイル ライセンス アクション
BMC2024_Nakagawa.pdf BMC2024_Nakagawa.pdf (1.3 MB)
 Download is available from 2026/5/1.
アイテムタイプ itemtype_ver1(1)
公開日 2024-10-16
タイトル
タイトル Molecular basis of N-glycan recognition by pradimicin a and its potential as a SARS-CoV-2 entry inhibitor
言語 en
著者 Nakagawa, Yu

× Nakagawa, Yu

en Nakagawa, Yu

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Fujii, Masato

× Fujii, Masato

en Fujii, Masato

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Ito, Nanaka

× Ito, Nanaka

en Ito, Nanaka

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Ojika, Makoto

× Ojika, Makoto

en Ojika, Makoto

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Akase, Dai

× Akase, Dai

en Akase, Dai

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Aida, Misako

× Aida, Misako

en Aida, Misako

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Kinoshita, Takaaki

× Kinoshita, Takaaki

en Kinoshita, Takaaki

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Sakurai, Yasuteru

× Sakurai, Yasuteru

en Sakurai, Yasuteru

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Yasuda, Jiro

× Yasuda, Jiro

en Yasuda, Jiro

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Igarashi, Yasuhiro

× Igarashi, Yasuhiro

en Igarashi, Yasuhiro

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Ito, Yukishige

× Ito, Yukishige

en Ito, Yukishige

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アクセス権
アクセス権 embargoed access
アクセス権URI http://purl.org/coar/access_right/c_f1cf
権利
権利情報 © 2024. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
言語 en
内容記述
内容記述タイプ Abstract
内容記述 Virus entry inhibitors are emerging as an attractive class of therapeutics for the suppression of viral transmission. Naturally occurring pradimicin A (PRM-A) has received particular attention as the first-in-class entry inhibitor that targets N-glycans present on viral surface. Despite the uniqueness of its glycan-targeted antiviral activity, there is still limited knowledge regarding how PRM-A binds to viral N-glycans. Therefore, in this study, we performed binding analysis of PRM-A with synthetic oligosaccharides that reflect the structural motifs characteristic of viral N-glycans. Binding assays and molecular modeling collectively suggest that PRM-A preferentially binds to branched oligomannose motifs of N-glycans via simultaneous recognition of two mannose residues at the non-reducing ends. We also demonstrated, for the first time, that PRM-A can effectively inhibit severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection in vitro. Significantly, the anti-SARS-CoV-2 effect of PRM-A is attenuated in the presence of the synthetic branched oligomannose, suggesting that the inhibition of SARS-CoV-2 infection is due to the interaction of PRM-A with the branched oligomannose-containing N-glycans. These data provide essential information needed to understand the antiviral mechanism of PRM-A and suggest that PRM-A could serve as a candidate SARS-CoV-2 entry inhibitor targeting N-glycans.
言語 en
出版者
出版者 Elsevier
言語 en
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
関連情報
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.bmc.2024.117732
収録物識別子
収録物識別子タイプ PISSN
収録物識別子 09680896
書誌情報 en : Bioorganic & Medicinal Chemistry

巻 105, p. 117732, 発行日 2024-05-01
ファイル公開日
日付 2026-05-01
日付タイプ Available
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