Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans

Influenza 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...

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Autores: Canales, Ángeles, Sastre, Javier, Orduña, José María, Spruit, Cindy M., Pérez Castells, Javier, Domínguez, Gema, Bouwman, Kim M., van der Woude, Roosmarijn, Cañada Vicinay, Francisco Javier, Nycholat, Corwin M., Paulson, James C., Boons, Geert-Jan, Jiménez Barbero, Jesús, de Vries, Robert P.
Tipo de recurso: artículo
Fecha de publicación:2023
País:España
Institución:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/60920
Acceso en línea:http://hdl.handle.net/10810/60920
Access Level:acceso abierto
Palabra clave:influenza virus
N-glycan
recognition
glycan array
NMR
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spelling Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-GlycansCanales, ÁngelesSastre, JavierOrduña, José MaríaSpruit, Cindy M.Pérez Castells, JavierDomínguez, GemaBouwman, Kim M.van der Woude, RoosmarijnCañada Vicinay, Francisco JavierNycholat, Corwin M.Paulson, James C.Boons, Geert-JanJiménez Barbero, Jesúsde Vries, Robert P.influenza virusN-glycanrecognitionglycan arrayNMRInfluenza 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.R.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.American Chemical SocietyEuropean Commission202320232023info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/60920reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoInglésinfo:eu-repo/grantAgreement/EC/ERC/802780info:eu-repo/grantAgreement/MICINN/PID2019-105237GB-I00/info:eu-repo/grantAgreement/MICIU/RTI2018-095588-B-I00/info:eu-repo/grantAgreement/EC/ERC/788143info:eu-repo/grantAgreement/MICIU/RTI2018-094751-B-C21/info:eu-repo/grantAgreement/MICIU/RTI2018-094751-B-C22/info:eu-repo/grantAgreement/MICINN/PDI2021-1237810B-C21/info:eu-repo/grantAgreement/MICINN/PDI2021-1237810B-C22/https://pubs.acs.org/doi/10.1021/jacsau.2c00664info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/3.0/es/© 2023 The Authors. Published by American Chemical Society. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)Atribución-NoComercial-SinDerivadas 3.0 Españaoai:addi.ehu.eus:10810/609202026-06-18T09:23:17Z
dc.title.none.fl_str_mv Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
title Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
spellingShingle Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
Canales, Ángeles
influenza virus
N-glycan
recognition
glycan array
NMR
title_short Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
title_full Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
title_fullStr Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
title_full_unstemmed Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
title_sort Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
dc.creator.none.fl_str_mv Canales, Ángeles
Sastre, Javier
Orduña, José María
Spruit, Cindy M.
Pérez Castells, Javier
Domínguez, Gema
Bouwman, Kim M.
van der Woude, Roosmarijn
Cañada Vicinay, Francisco Javier
Nycholat, Corwin M.
Paulson, James C.
Boons, Geert-Jan
Jiménez Barbero, Jesús
de Vries, Robert P.
author Canales, Ángeles
author_facet Canales, Ángeles
Sastre, Javier
Orduña, José María
Spruit, Cindy M.
Pérez Castells, Javier
Domínguez, Gema
Bouwman, Kim M.
van der Woude, Roosmarijn
Cañada Vicinay, Francisco Javier
Nycholat, Corwin M.
Paulson, James C.
Boons, Geert-Jan
Jiménez Barbero, Jesús
de Vries, Robert P.
author_role author
author2 Sastre, Javier
Orduña, José María
Spruit, Cindy M.
Pérez Castells, Javier
Domínguez, Gema
Bouwman, Kim M.
van der Woude, Roosmarijn
Cañada Vicinay, Francisco Javier
Nycholat, Corwin M.
Paulson, James C.
Boons, Geert-Jan
Jiménez Barbero, Jesús
de Vries, Robert P.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv European Commission
dc.subject.none.fl_str_mv influenza virus
N-glycan
recognition
glycan array
NMR
topic influenza virus
N-glycan
recognition
glycan array
NMR
description Influenza 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.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/60920
url http://hdl.handle.net/10810/60920
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/EC/ERC/802780
info:eu-repo/grantAgreement/MICINN/PID2019-105237GB-I00/
info:eu-repo/grantAgreement/MICIU/RTI2018-095588-B-I00/
info:eu-repo/grantAgreement/EC/ERC/788143
info:eu-repo/grantAgreement/MICIU/RTI2018-094751-B-C21/
info:eu-repo/grantAgreement/MICIU/RTI2018-094751-B-C22/
info:eu-repo/grantAgreement/MICINN/PDI2021-1237810B-C21/
info:eu-repo/grantAgreement/MICINN/PDI2021-1237810B-C22/
https://pubs.acs.org/doi/10.1021/jacsau.2c00664
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
Atribución-NoComercial-SinDerivadas 3.0 España
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/3.0/es/
Atribución-NoComercial-SinDerivadas 3.0 España
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:Addi. Archivo Digital para la Docencia y la Investigación
instname:Universidad del País Vasco
instname_str Universidad del País Vasco
reponame_str Addi. Archivo Digital para la Docencia y la Investigación
collection Addi. Archivo Digital para la Docencia y la Investigación
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.300719

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