Influenza binds phosphorylated glycans from human lung

• Type of Material: Article
• Authors: Lauren Byrd-Leotis, Emory University; Nan Jia, Harvard Medical School; Sucharita Dutta, Harvard Medical School; Jessica F. Trost, Emory University; Chao Gao, Harvard Medical School; Sandra F. Cummings, Harvard Medical Center; Thomas Braulke, University Medical Center Hamburg-Eppendorf; Sven Mueller-Loennies, Leibniz Lung Center; Jamie Heimburg-Molinaro, Harvard Medical School; David Steinhauer, Emory University; Richard Cummings, Emory University
• Language: English
• Date: 2019-02-01
• Publisher: American Association for the Advancement of Science: Science Advances
• Publication Version: Final Published Version
• Copyright Statement: © 2019 The Authors.
• License: Creative Commons Attribution-NonCommercial 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1126/sciadv.aav2554
• Title of Journal or Parent Work: Science Advances
• ISSN: 2375-2548
• Volume: 5
• Issue: 2
• Start Page: eaav2554
• End Page: eaav2554
• Grant/Funding Information: We acknowledge support by the U.S. Department of Health and Human Services contract HHSN272201400004C (NIAID Centers of Excellence for Influenza Research and Surveillance) and the NIH award P41GM103694 (National Center for Functional Glycomics).; J.F.T. was supported by National Institute of Allergy and Infectious Disease (NIAID) of the NIH under award number T32AI106699.
• Keywords: SHOTGUN GLYCOMICS; CELL; HEMAGGLUTININS; Science & Technology - Other Topics; OLIGOSACCHARIDES; TRANSMISSION; Science & Technology; INFECTION; MICROARRAY STRATEGY; RECEPTOR-BINDING; SPECIFICITY; VIRUS; Multidisciplinary Sciences
• Research Categories: Biology, Microbiology; Chemistry, Biochemistry; Health Sciences, Immunology

Abstract

Influenza A viruses can bind sialic acid–terminating glycan receptors, and species specificity is often correlated with sialic acid linkage with avian strains recognizing 2,3-linked sialylated glycans and mammalian strains preferring 2,6-linked sialylated glycans. These paradigms derive primarily from studies involving erythrocyte agglutination, binding to synthetic receptor analogs or binding to undefined surface markers on cells or tissues. Here, we present the first examination of the N-glycome of the human lung for identifying natural receptors for a range of avian and mammalian influenza viruses. We found that the human lung contains many 2,3- and 2,6-linked sialylated glycan determinants bound by virus, but all viruses also bound to phosphorylated, nonsialylated glycans.