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dc.contributor.authorSassaki, Guilherme L.
dc.contributor.authorElli, Stefano
dc.contributor.authorRudd, Timothy R.
dc.contributor.authorMacchi, Eleonora
dc.contributor.authorYates, Edwin A.
dc.contributor.authorNaggi, Annamaria
dc.contributor.authorRaman, Rahul
dc.contributor.authorTorri, Giangiacomo
dc.contributor.authorGuerrini, Marco
dc.contributor.authorShriver, Zachary H.
dc.contributor.authorSasisekharan, Ram
dc.date.accessioned2015-10-29T18:47:00Z
dc.date.available2015-10-29T18:47:00Z
dc.date.issued2013-09
dc.date.submitted2013-09
dc.identifier.issn0006-2960
dc.identifier.issn1520-4995
dc.identifier.urihttp://hdl.handle.net/1721.1/99521
dc.description.abstractDifferential interactions between influenza A virus protein hemagglutinin (HA) and α2→3 (avian) or α2→6 (human) sialylated glycan receptors play an important role in governing host specificity and adaptation of the virus. Previous analysis of HA–glycan interactions with trisaccharides showed that, in addition to the terminal sialic acid linkage, the conformation and topology of the glycans, while they are bound to HA, are key factors in regulating these interactions. Here, the solution conformation and dynamics of two representative avian and human glycan pentasaccharide receptors [LSTa, Neu5Ac-α(2→3)-Gal-β(1→3)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc; LSTc, (Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc] have been explored using nuclear magnetic resonance and molecular dynamics simulation. Analyses demonstrate that, in solution, human and avian receptors sample distinct conformations, topologies, and dynamics. These unique features of avian and human receptors in solution could represent distinct molecular characteristics for recognition by HA, thereby providing the HA–glycan interaction specificity in influenza.en_US
dc.description.sponsorshipFinlombardia SPAen_US
dc.description.sponsorshipConselho Nacional de Pesquisas (Brazil)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (R37 GM057073-13)en_US
dc.description.sponsorshipSingapore. National Research Foundation (Singapore-MIT Alliance for Research and Technology)en_US
dc.language.isoen_US
dc.publisherAmerican Chemical Society (ACS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/bi400677nen_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourcePMCen_US
dc.titleHuman (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solutionen_US
dc.typeArticleen_US
dc.identifier.citationSassaki, Guilherme L., Stefano Elli, Timothy R. Rudd, Eleonora Macchi, Edwin A. Yates, Annamaria Naggi, Zachary Shriver, et al. “Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution.” Biochemistry 52, no. 41 (October 15, 2013): 7217–7230.en_US
dc.contributor.departmentHarvard University--MIT Division of Health Sciences and Technologyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. School of Engineeringen_US
dc.contributor.departmentKoch Institute for Integrative Cancer Research at MITen_US
dc.contributor.mitauthorShriver, Zachary H.en_US
dc.contributor.mitauthorRaman, Rahulen_US
dc.contributor.mitauthorSasisekharan, Ramen_US
dc.relation.journalBiochemistryen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsSassaki, Guilherme L.; Elli, Stefano; Rudd, Timothy R.; Macchi, Eleonora; Yates, Edwin A.; Naggi, Annamaria; Shriver, Zachary; Raman, Rahul; Sasisekharan, R.; Torri, Giangiacomo; Guerrini, Marcoen_US
dc.identifier.orcidhttps://orcid.org/0000-0001-9344-0205
dc.identifier.orcidhttps://orcid.org/0000-0002-2085-7840
mit.licensePUBLISHER_POLICYen_US


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