4edb
From Proteopedia
Structures of monomeric hemagglutinin and its complex with an Fab fragment of a neutralizing antibody that binds to H1 subtype influenza viruses: molecular basis of infectivity of 2009 pandemic H1N1 influenza A viruses
Structural highlights
Function[A7LI25_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS001364_004_327643] Publication Abstract from PubMedInfluenza virus infects host cells through membrane fusion, a process mediated by the low pH-induced conformational change of the viral surface glycoprotein hemagglutinin (HA). We determined the structures and biochemical properties of the HA proteins from A/Korea/01/2009 (KR01), a 2009 pandemic strain, and A/Thailand/CU44/2006 (CU44), a seasonal strain. The crystal structure of KR01 HA revealed a V-shaped head-to-head arrangement, which is not seen in other HA proteins including CU44 HA. We isolated a broadly neutralizing H1-specific monoclonal antibody GC0757. The KR01 HA-Fab0757 complex structure also exhibited a head-to-head arrangement of HA. Both native and Fab complex structures reveal different spatial orientation of HA1 relative to HA2, indicating that HA is flexible and dynamic at neutral pH. Further, the KR01 HA exhibited significantly lower protein stability and increased susceptibility to proteolytic cleavage compared with other HAs. Our structures provide important insight into conformational flexibility of HA. Insight into structural diversity of influenza virus hemagglutinin.,Cho KJ, Lee JH, Hong KW, Kim SH, Park Y, Lee JY, Kang S, Kim S, Yang JH, Kim EK, Seok JH, Unzai S, Park SY, Saelens X, Kim CJ, Lee JY, Kang C, Oh HB, Chung MS, Kim KH J Gen Virol. 2013 May 1. PMID:23636824[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Large Structures | Alam I | Cho KJ | Kang SH | Khan TG | Kim KH | Lee JH | Lee JY | Park YH
