Divalent cation-induced conformational changes of influenza virus hemagglutinin.

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 stabil

SUBMITTER: Seok JH 

PROVIDER: S-EPMC7508890 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature