Year: 2017
Type: article
Abstract: The avian H7N9 influenza outbreak in 2013 resulted from an unprecedented incidence of influenza transmission to humans from infected poultry.The majority of human H7N9 isolates contained a hemagglutinin (HA) mutation (Q226L) that has previously been associated with a switch in receptor specificity from avian-type (NeuAcα2-3Gal) to human-type (NeuAcα2-6Gal), as documented for the avian progenitors of the 1957 (H2N2) and 1968 (H3N2) human influenza pandemic viruses.While this raised concern that the H7N9 virus was adapting to humans, the mutation was not sufficient to switch the receptor specificity of H7N9, and has not resulted in sustained transmission in humans.To determine if the H7 HA was capable of acquiring human-type receptor specificity, we conducted mutation analyses.Remarkably, three amino acid mutations conferred a switch in specificity for human-type receptors that resembled the specificity of the 2009 human H1 pandemic virus, and promoted binding to human trachea epithelial cells. Author summaryInfluenza A virus of the H7N9 subtype continues to cross the species barrier from poultry to humans.This zoonotic ability is remarkable as the virus retains specificity to aviantype receptors.To effectively transmit between humans, the virus needs to acquire human-type receptor specificity.In this study, we show that recombinant H7 proteins
Source: PLoS Pathogens
Authors: Robert P. de Vries, Wenjie Peng, Oliver C. Grant, Andrew J. Thompson, Xueyong Zhu, Kim M. Bouwman, Alba T. Torrents de la Pena, Marielle J. van Breemen, Iresha N. Ambepitiya Wickramasinghe, Cornelis A. M. de Haan, Wenli Yu, Ryan McBride, Rogier W. Sanders, Robert J. Woods, Monique H. Verheije, Ian A. Wilson, James C. Paulson
Language: English
Subfield: Epidemiology
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $3,043
Funders: U.S. Department of Energy, European Molecular Biology Organization, Universiteit Utrecht, Nederlandse Organisatie voor Wetenschappelijk Onderzoek, National Institutes of Health, Centers for Disease Control and Prevention, Office of Science, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, National Center for Research Resources, Basic Energy Sciences, Biological and Environmental Research
Awards: G102163711, G1027097336, G113944070, G1286251239, G1384768361, G1710779858, G1804828992, G1831385526, G2219523378, G222407312, G2287611682, G2300450775, G2363639003, G2483123008, G262962599, Continued Development and Maintenance of GLYCAM-Web, G2849562071, G2857925935, G3152346458, G3244038948, G3351052168, G3488436650, Exploiting sites of vulnerability on influenza viruses, G3629260272, G3878151401, G402281873, G409777406, G4259240498, G426311843, G4312656029, G4385809619, G4503765041, G4597657575, G4727740710, G4847693919, G4866076653, G498139845, G5176655522, Resource for Integrated Glycotechnology, G5368254702, G5387317844, G5607048534, G6004781752, G6848031779, G6918803902, G7186539832, G7210391181, G7374214904, G7583137537, G7688398576, A Synchroton Radiation Structural Biology Resource, G9000028044, G9000069621, G9000138594, G9000163281, G9000208973, G9000333702, G969889393, G993149817
OpenAlex ID: W2625936141