6LKS

Effects of zinc ion on oligomerization and pH stability of influenza virus hemagglutinin

Summary for 6LKS

• Entry DOI: 10.2210/pdb6lks/pdb
• Descriptor: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: zinc induced the oligomerization, viral membrane protein, ph induced conformational change, viral protein
• Biological source: Influenza A virus (A/Thailand/CU44/2006(H1N1)); More
• Total number of polymer chains: 12
• Total formula weight: 359731.56

Authors

Seok, J.,Kim, K. (deposition date: 2019-12-20, release date: 2020-10-21, Last modification date: 2024-10-23)

Primary citation

Seok, J.H.,Kim, H.,Lee, D.B.,An, J.S.,Kim, E.J.,Lee, J.H.,Chung, M.S.,Kim, K.H.
Divalent cation-induced conformational changes of influenza virus hemagglutinin.
Sci Rep, 10:15457-15457, 2020

PubMed Abstract: Divalent cations Cu and Zn 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 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 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. 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 may facilitate the conformational changes of HA, analogous to that induced by acidic pH.

PubMed: 32963316
DOI: 10.1038/s41598-020-72368-x

Experimental method

X-RAY DIFFRACTION (3.24 Å)