6twi | pdb_00006twi

Crystal structure of the haemagglutinin mutant (Gln226Leu, Gly228Ser) from an H10N7 seal influenza virus isolated in Germany in complex with avian receptor analogue 3'-SLN

spinqualitylabelsall models 6twi, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6twi is a 6 chain structure with sequence from Influenza A virus (A/harbour seal/Germany/1/2014(H10N7)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Ligands: CA, EDO, GAL, NAG, PRD_900067, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0A7HR51_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.[RuleBase:RU003324] Publication Abstract from PubMed In 2014, an outbreak of avian A/H10N7 influenza virus occurred among seals along North-European coastal waters, significantly impacting seal populations. Here, we examine the cross-species transmission and mammalian adaptation of this influenza A virus, revealing changes in the hemagglutinin surface protein that increase stability and receptor binding. The seal A/H10N7 virus was aerosol or respiratory droplet transmissible between ferrets. Compared with avian H10 hemagglutinin, seal H10 hemagglutinin showed stronger binding to the human-type sialic acid receptor, with preferential binding to alpha2,6-linked sialic acids on long extended branches. In X-ray structures, changes in the 220-loop of the receptor-binding pocket caused similar interactions with human receptor as seen for pandemic strains. Two substitutions made seal H10 hemagglutinin more stable than avian H10 hemagglutinin and similar to human hemagglutinin. Consequently, identification of avian-origin influenza viruses across mammals appears critical to detect influenza A viruses posing a major threat to humans and other mammals. Hemagglutinin Traits Determine Transmission of Avian A/H10N7 Influenza Virus between Mammals.,Herfst S, Zhang J, Richard M, McBride R, Lexmond P, Bestebroer TM, Spronken MIJ, de Meulder D, van den Brand JM, Rosu ME, Martin SR, Gamblin SJ, Xiong X, Peng W, Bodewes R, van der Vries E, Osterhaus ADME, Paulson JC, Skehel JJ, Fouchier RAM Cell Host Microbe. 2020 Oct 7;28(4):602-613.e7. doi: 10.1016/j.chom.2020.08.011. PMID:33031770 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemagglutinin 3D structures

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