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dc.contributor.authorSrinivasan, Karunya
dc.contributor.authorRaman, Rahul
dc.contributor.authorJayaraman, Akila
dc.contributor.authorViswanathan, Karthik
dc.contributor.authorSasisekharan, Ram
dc.date.accessioned2018-09-11T15:50:12Z
dc.date.available2018-09-11T15:50:12Z
dc.date.issued2013-02
dc.date.submitted2012-06
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/1721.1/117714
dc.description.abstractIn the context of recently emerged novel influenza strains through reassortment, avian influenza subtypes such as H5N1, H7N7, H7N2, H7N3 and H9N2 pose a constant threat in terms of their adaptation to the human host. Among these subtypes, it was recently demonstrated that mutations in H5 and H9 hemagglutinin (HA) in the context of lab-generated reassorted viruses conferred aerosol transmissibility in ferrets (a property shared by human adapted viruses). We previously demonstrated that the quantitative binding affinity of HA to α2→6 sialylated glycans (human receptors) is one of the important factors governing human adaptation of HA. Although the H7 subtype has infected humans causing varied clinical outcomes from mild conjunctivitis to severe respiratory illnesses, it is not clear where the HA of these subtypes stand in regard to human adaptation since its binding affinity to glycan receptors has not yet been quantified. In this study, we have quantitatively characterized the glycan receptor-binding specificity of HAs from representative strains of Eurasian (H7N7) and North American (H7N2) lineages that have caused human infection. Furthermore, we have demonstrated for the first time that two specific mutations; Gln226→Leu and Gly228→Ser in glycan receptor-binding site of H7 HA substantially increase its binding affinity to human receptor. Our findings contribute to a framework for monitoring the evolution of H7 HA to be able to adapt to human host.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant R37057073-13)en_US
dc.publisherPublic Library of Science (PLoS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1371/JOURNAL.PONE.0049597en_US
dc.rightsCreative Commons Attribution 4.0 International Licenseen_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.sourcePLoSen_US
dc.titleQuantitative Description of Glycan-Receptor Binding of Influenza A Virus H7 Hemagglutininen_US
dc.typeArticleen_US
dc.identifier.citationSrinivasan, Karunya et al. “Quantitative Description of Glycan-Receptor Binding of Influenza A Virus H7 Hemagglutinin.” Edited by Earl G. Brown. PLoS ONE 8, 2 (February 2013): e49597 © 2013 Srinivasan et alen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.departmentKoch Institute for Integrative Cancer Research at MITen_US
dc.contributor.mitauthorSrinivasan, Karunya
dc.contributor.mitauthorRaman, Rahul
dc.contributor.mitauthorJayaraman, Akila
dc.contributor.mitauthorViswanathan, Karthik
dc.contributor.mitauthorSasisekharan, Ram
dc.relation.journalPLoS ONEen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2018-09-10T19:20:12Z
dspace.orderedauthorsSrinivasan, Karunya; Raman, Rahul; Jayaraman, Akila; Viswanathan, Karthik; Sasisekharan, Ramen_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-1288-9965
dc.identifier.orcidhttps://orcid.org/0000-0002-2085-7840
mit.licensePUBLISHER_CCen_US


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