6ty1
From Proteopedia
Crystal structure of the haemagglutinin mutant (Gln226Leu, Gly228Ser) from an H10N7 seal influenza virus isolated in Germany in complex with human receptor analogue 6'-SLN
Structural highlights
Publication Abstract from PubMedIn 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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Categories: Large Structures | Gamblin S | Purkiss A | Skehel JJ | Walker P | Xiong X | Zhang J