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Publication Abstract from PubMed

Divalent cations Cu(2+) and Zn(2+) 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 Zn(2+) 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 Zn(2+) 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 Zn(2+). 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 Zn(2+) may facilitate the conformational changes of HA, analogous to that induced by acidic pH.

Divalent cation-induced conformational changes of influenza virus hemagglutinin.,Seok JH, Kim H, Lee DB, An JS, Kim EJ, Lee JH, Chung MS, Kim KH Sci Rep. 2020 Sep 22;10(1):15457. doi: 10.1038/s41598-020-72368-x. PMID:32963316^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.