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

DOI: 10.1016/j.chom.2020.08.011

Authors: Sander Herfst (Erasmus MC University Medical Center) , Jie Zhang (Francis Crick Institute (Midland Road)) , Mathilde Richard (Erasmus MC University Medical Center) , Ryan Mcbride (Scripps Research Institute) , Pascal Lexmond (Erasmus MC University Medical Center) , Theo M. Bestebroer (Erasmus MC University Medical Center) , Monique I. J. Spronken (Erasmus MC University Medical Center) , Dennis De Meulder (Erasmus MC University Medical Center) , Judith M. Van Den Brand (Erasmus MC University Medical Center) , Miruna E. Rosu (Erasmus MC University Medical Center) , Stephen R. Martin (Francis Crick Institute) , Steven J. Gamblin (Francis Crick Institute) , Xiaoli Xiong (Francis Crick Institute) , Wenjie Peng (Scripps Research Institute) , Rogier Bodewes (Erasmus MC University Medical Center) , Erhard Van Der Vries (Erasmus MC University Medical Center) , Albert D. M. E. Osterhaus (University of Veterinary Medicine) , James C. Paulson (Scripps Research Institute) , John J. Skehel (Francis Crick Institute) , Ron A. M. Fouchier (Erasmus MC University Medical Center)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell Host & Microbe , VOL 28 , PAGES 602 - 613.e7

State: Published (Approved)
Published: October 2020
Diamond Proposal Number(s): 9826 , 13775

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.

Journal Keywords: influenza; A/H10N7; transmission; aerosol; respiratory droplet; hemagglutinin; receptor-binding; stability; glycan microarrays

Diamond Keywords: Avian Flu; Viruses

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography

Added On: 14/10/2020 08:46

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech Veterinary Medicine

Technical Tags:

Diffraction Macromolecular Crystallography (MX)