Divalent cation-induced conformational changes of influenza virus hemagglutinin
DC Field | Value | Language |
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dc.contributor.author | Seok, Jong Hyeon | - |
dc.contributor.author | Kim, Hyojin | - |
dc.contributor.author | Lee, Dan Bi | - |
dc.contributor.author | An, Jeong Suk | - |
dc.contributor.author | Kim, Eun Jeong | - |
dc.contributor.author | Lee, Ji-Hye | - |
dc.contributor.author | Chung, Mi Sook | - |
dc.contributor.author | Kim, Kyung Hyun | - |
dc.date.accessioned | 2021-08-30T13:59:57Z | - |
dc.date.available | 2021-08-30T13:59:57Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2020-09-22 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/53119 | - |
dc.description.abstract | Divalent cations Cu2+ and Zn2+ can prevent the viral growth in mammalian cells during influenza infection, and viral titers decrease significantly on a copper surface. The underlying mechanisms include DNA damage by radicals, modulation of viral protease, M1 or neuraminidase, and morphological changes in viral particles. However, the molecular mechanisms underlying divalent cation-mediated antiviral activities are unclear. An unexpected observation of this study was that a Zn2+ ion is bound by Glu68 and His137 residues at the head regions of two neighboring trimers in the crystal structure of hemagglutinin (HA) derived from A/Thailand/CU44/2006. The binding of Zn2+ at high concentrations induced multimerization of HA and decreased its acid stability. The acid-induced conformational change of HA occurred even at neutral pH in the presence of Zn2+. The fusion of viral and host endosomal membranes requires substantial conformational changes in HA upon exposure to acidic pH. Therefore, our results suggest that binding of Zn2+ may facilitate the conformational changes of HA, analogous to that induced by acidic pH. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE RESEARCH | - |
dc.subject | RECEPTOR-BINDING | - |
dc.subject | ZINC TOXICITY | - |
dc.subject | A VIRUS | - |
dc.subject | FUSION | - |
dc.subject | PH | - |
dc.subject | STABILITY | - |
dc.subject | REGION | - |
dc.subject | COPPER | - |
dc.subject | INACTIVATION | - |
dc.subject | PROTEINS | - |
dc.title | Divalent cation-induced conformational changes of influenza virus hemagglutinin | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Kyung Hyun | - |
dc.identifier.doi | 10.1038/s41598-020-72368-x | - |
dc.identifier.scopusid | 2-s2.0-85091279727 | - |
dc.identifier.wosid | 000577219100006 | - |
dc.identifier.bibliographicCitation | SCIENTIFIC REPORTS, v.10, no.1 | - |
dc.relation.isPartOf | SCIENTIFIC REPORTS | - |
dc.citation.title | SCIENTIFIC REPORTS | - |
dc.citation.volume | 10 | - |
dc.citation.number | 1 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | RECEPTOR-BINDING | - |
dc.subject.keywordPlus | ZINC TOXICITY | - |
dc.subject.keywordPlus | A VIRUS | - |
dc.subject.keywordPlus | FUSION | - |
dc.subject.keywordPlus | PH | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | REGION | - |
dc.subject.keywordPlus | COPPER | - |
dc.subject.keywordPlus | INACTIVATION | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordAuthor | influenza virus | - |
dc.subject.keywordAuthor | hemagglutinin | - |
dc.subject.keywordAuthor | metal ion effect | - |
dc.subject.keywordAuthor | pH-dependent conformations | - |
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