Divalent cation-induced conformational changes of influenza virus hemagglutinin
- Authors
- Seok, Jong Hyeon; Kim, Hyojin; Lee, Dan Bi; An, Jeong Suk; Kim, Eun Jeong; Lee, Ji-Hye; Chung, Mi Sook; Kim, Kyung Hyun
- Issue Date
- 22-9월-2020
- Publisher
- NATURE RESEARCH
- Keywords
- influenza virus; hemagglutinin; metal ion effect; pH-dependent conformations
- Citation
- SCIENTIFIC REPORTS, v.10, no.1
- Indexed
- SCIE
SCOPUS
- Journal Title
- SCIENTIFIC REPORTS
- Volume
- 10
- Number
- 1
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/53119
- DOI
- 10.1038/s41598-020-72368-x
- ISSN
- 2045-2322
- 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.
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Collections - Graduate School > Department of Biotechnology and Bioinformatics > 1. Journal Articles
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