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dc.contributor.authorCanales, Ángeles
dc.contributor.authorSastre, Javier
dc.contributor.authorOrduña, José María
dc.contributor.authorSpruit, Cindy M.
dc.contributor.authorPérez Castells, Javier
dc.contributor.authorDomínguez, Gema
dc.contributor.authorBouwman, Kim M.
dc.contributor.authorvan der Woude, Roosmarijn
dc.contributor.authorCañada Vicinay, Francisco Javier
dc.contributor.authorNycholat, Corwin M.
dc.contributor.authorPaulson, James C.
dc.contributor.authorBoons, Geert-Jan
dc.contributor.authorJiménez Barbero, Jesús ORCID
dc.contributor.authorde Vries, Robert P.
dc.date.accessioned2023-04-24T17:38:45Z
dc.date.available2023-04-24T17:38:45Z
dc.date.issued2023-02
dc.identifier.citationJACS Au 3(3) : 868-878 (2023)es_ES
dc.identifier.issn2691-3704
dc.identifier.urihttp://hdl.handle.net/10810/60920
dc.description.abstractInfluenza virus infection remains a threat to human health since viral hemagglutinins are constantly drifting, escaping infection and vaccine-induced antibody responses. Viral hemag-glutinins from different viruses display variability in glycan recognition. In this context, recent H3N2 viruses have specificity for alpha 2,6 sialylated branched N-glycans with at least three N- acetyllactosamine units (tri-LacNAc). In this work, we combined glycan arrays and tissue binding analyses with nuclear magnetic resonance experiments to characterize the glycan specificity of a family of H1 variants, including the one responsible for the 2009 pandemic outbreak. We also analyzed one engineered H6N1 mutant to understand if the preference for tri-LacNAc motifs could be a general trend in human-type receptor-adapted viruses. In addition, we developed a new NMR approach to perform competition experiments between glycans with similar compositions and different lengths. Our results point out that pandemic H1 viruses differ from previous seasonal H1 viruses by a strict preference for a minimum of di-LacNAc structural motifs.es_ES
dc.description.sponsorshipR.P.d.V. is a recipient of an ERC Starting grant from the European Commission (802780) and a Beijerinck Premium of the Royal Dutch Academy of Sciences. The glycan array setup was supported by the Netherlands Organization for Scientific Research (NWO, TOP-PUNT 718.015.003 to G.-J.P.H.B.). Dr. Lin Liu (CCRC) and Dr. Margreet A . Wolfert (Utrecht University) developed, printed, and validated the glycan microarray. We would like to thank Nikoloz Nemanichvili for technical assistance. A.C. acknowledges funding from Agencia Estatal de Investigacion "Spanish Ministry of Science and Innovation" (MICINN) project PID2019-105237GB-I00. J.P.C. acknowledges funding by the Spanish MICINN, grant no. RTI2018-095588-B-I00 (co-funded by the European Regional Development Fund/European Social Fund, "Invest-ing in your future"). JJB also tha n k s funding by the European Research Council (RECGLYCANMR, Advanced grant no. 788143), the Agencia Estatal de Investigacion (Spain) for grants RTI2018-094751-B-C21 and C22 and PDI2021-1237810B-C21 and C22, and CIBERES, an initiative of the Instituto de Salud Carlos III (ISCIII), Madrid, Spain. The NMR spectra were acquired at the NMR service of CIBMargarita Salas and in the NMR faci l i t y of the UCM. We also acknowledge Prof. Robert Woods group for sending us the coordinates of a glycan-hemagglut i n i n model.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Chemical Societyes_ES
dc.relationinfo:eu-repo/grantAgreement/EC/ERC/802780es_ES
dc.relationinfo:eu-repo/grantAgreement/MICINN/PID2019-105237GB-I00es_ES
dc.relationinfo:eu-repo/grantAgreement/MICIU/RTI2018-095588-B-I00es_ES
dc.relationinfo:eu-repo/grantAgreement/EC/ERC/788143es_ES
dc.relationinfo:eu-repo/grantAgreement/MICIU/RTI2018-094751-B-C21es_ES
dc.relationinfo:eu-repo/grantAgreement/MICIU/RTI2018-094751-B-C22es_ES
dc.relationinfo:eu-repo/grantAgreement/MICINN/PDI2021-1237810B-C21es_ES
dc.relationinfo:eu-repo/grantAgreement/MICINN/PDI2021-1237810B-C22es_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.subjectinfluenza viruses_ES
dc.subjectN-glycanes_ES
dc.subjectrecognitiones_ES
dc.subjectglycan arrayes_ES
dc.subjectNMRes_ES
dc.titleRevealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycanses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.holder© 2023 The Authors. Published by American Chemical Society. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)es_ES
dc.rights.holderAtribución-NoComercial-SinDerivadas 3.0 España*
dc.relation.publisherversionhttps://pubs.acs.org/doi/10.1021/jacsau.2c00664es_ES
dc.identifier.doi10.1021/jacsau.2c00664
dc.contributor.funderEuropean Commission
dc.departamentoesQuímica Orgánica e Inorgánicaes_ES
dc.departamentoeuKimika Organikoa eta Ez-Organikoaes_ES


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© 2023 The Authors. Published by American Chemical Society. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
Except where otherwise noted, this item's license is described as © 2023 The Authors. Published by American Chemical Society. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)