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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I03-Macromolecular Crystallography	Hemagglutinin traits determine transmission of avian A/H10N7 influenza virus between mammals Sander Herfst , Jie Zhang , Mathilde Richard , Ryan Mcbride , Pascal Lexmond , Theo M. Bestebroer , Monique I. J. Spronken , Dennis De Meulder , Judith M. Van Den Brand , Miruna E. Rosu , Stephen R. Martin , Steven J. Gamblin , Xiaoli Xiong , Wenjie Peng , Rogier Bodewes , Erhard Van Der Vries , Albert D. M. E. Osterhaus , James C. Paulson , John J. Skehel , Ron A. M. Fouchier Cell Host & Microbe 28, 602 - 613.e7 DOI: 10.1016/j.chom.2020.08.011 Diamond Proposal Number(s): [9826, 13775] Show Abstract ▼ Abstract: 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 α2,6-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.	Oct 2020

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I02-Macromolecular Crystallography
I03-Macromolecular Crystallography

Hemagglutinin traits determine transmission of avian A/H10N7 influenza virus between mammals