Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs

Autores
Kosik, Ivan; Ince, William L.; Gentles, Lauren E.; Oler, Andrew J.; Kosikova, Martina; Angel, Matthew; Magadan, Javier Guillermo; Xie, Hang; Brooke, Christopher B.; Yewdell, Jonathan W.
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Rapid antigenic evolution enables the persistence of seasonal influenza A and B viruses in human populations despite widespread herd immunity. Understanding viral mechanisms that enable antigenic evolution is critical for designing durable vaccines and therapeutics. Here, we utilize the primerID method of error-correcting viral population sequencing to reveal an unexpected role for hemagglutinin (HA) glycosylation in compensating for fitness defects resulting from escape from anti-HA neutralizing antibodies. Antibody-free propagation following antigenic escape rapidly selected viruses with mutations that modulated receptor binding avidity through the addition of N-linked glycans to the HA globular domain. These findings expand our understanding of the viral mechanisms that maintain fitness during antigenic evolution to include glycan addition, and highlight the immense power of high-definition virus population sequencing to reveal novel viral adaptive mechanisms.
Fil: Kosik, Ivan. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Ince, William L.. National Institute of Allergy and Infectious Diseases; Estados Unidos. National Center For Toxicological Research. Food And Drug Administration; Estados Unidos
Fil: Gentles, Lauren E.. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Oler, Andrew J.. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Kosikova, Martina. National Center For Toxicological Research. Food And Drug Administration; Estados Unidos
Fil: Angel, Matthew. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Magadan, Javier Guillermo. National Institute of Allergy and Infectious Diseases; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Xie, Hang. National Center For Toxicological Research. Food And Drug Administration; Estados Unidos
Fil: Brooke, Christopher B.. University of Illinois at Urbana; Estados Unidos
Fil: Yewdell, Jonathan W.. National Institute of Allergy and Infectious Diseases; Estados Unidos
Materia
INFLUENZA
HEMAGGLUTININ
ANTIBODY ESCAPE
VIRAL EVOLUTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/91035
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/91035
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costsKosik, IvanInce, William L.Gentles, Lauren E.Oler, Andrew J.Kosikova, MartinaAngel, MatthewMagadan, Javier GuillermoXie, HangBrooke, Christopher B.Yewdell, Jonathan W.INFLUENZAHEMAGGLUTININANTIBODY ESCAPEVIRAL EVOLUTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Rapid antigenic evolution enables the persistence of seasonal influenza A and B viruses in human populations despite widespread herd immunity. Understanding viral mechanisms that enable antigenic evolution is critical for designing durable vaccines and therapeutics. Here, we utilize the primerID method of error-correcting viral population sequencing to reveal an unexpected role for hemagglutinin (HA) glycosylation in compensating for fitness defects resulting from escape from anti-HA neutralizing antibodies. Antibody-free propagation following antigenic escape rapidly selected viruses with mutations that modulated receptor binding avidity through the addition of N-linked glycans to the HA globular domain. These findings expand our understanding of the viral mechanisms that maintain fitness during antigenic evolution to include glycan addition, and highlight the immense power of high-definition virus population sequencing to reveal novel viral adaptive mechanisms.Fil: Kosik, Ivan. National Institute of Allergy and Infectious Diseases; Estados UnidosFil: Ince, William L.. National Institute of Allergy and Infectious Diseases; Estados Unidos. National Center For Toxicological Research. Food And Drug Administration; Estados UnidosFil: Gentles, Lauren E.. National Institute of Allergy and Infectious Diseases; Estados UnidosFil: Oler, Andrew J.. National Institute of Allergy and Infectious Diseases; Estados UnidosFil: Kosikova, Martina. National Center For Toxicological Research. Food And Drug Administration; Estados UnidosFil: Angel, Matthew. National Institute of Allergy and Infectious Diseases; Estados UnidosFil: Magadan, Javier Guillermo. National Institute of Allergy and Infectious Diseases; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Xie, Hang. National Center For Toxicological Research. Food And Drug Administration; Estados UnidosFil: Brooke, Christopher B.. University of Illinois at Urbana; Estados UnidosFil: Yewdell, Jonathan W.. National Institute of Allergy and Infectious Diseases; Estados UnidosPublic Library of Science2018-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/91035Kosik, Ivan; Ince, William L.; Gentles, Lauren E.; Oler, Andrew J.; Kosikova, Martina; et al.; Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs; Public Library of Science; Plos Pathogens; 14; 1; 1-2018; 1-19; e10067961553-7366CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.ppat.1006796info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006796info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:15:44Zoai:ri.conicet.gov.ar:11336/91035instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:15:44.624CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
title Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
spellingShingle Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
Kosik, Ivan
INFLUENZA
HEMAGGLUTININ
ANTIBODY ESCAPE
VIRAL EVOLUTION
title_short Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
title_full Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
title_fullStr Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
title_full_unstemmed Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
title_sort Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs
dc.creator.none.fl_str_mv Kosik, Ivan
Ince, William L.
Gentles, Lauren E.
Oler, Andrew J.
Kosikova, Martina
Angel, Matthew
Magadan, Javier Guillermo
Xie, Hang
Brooke, Christopher B.
Yewdell, Jonathan W.
author Kosik, Ivan
author_facet Kosik, Ivan
Ince, William L.
Gentles, Lauren E.
Oler, Andrew J.
Kosikova, Martina
Angel, Matthew
Magadan, Javier Guillermo
Xie, Hang
Brooke, Christopher B.
Yewdell, Jonathan W.
author_role author
author2 Ince, William L.
Gentles, Lauren E.
Oler, Andrew J.
Kosikova, Martina
Angel, Matthew
Magadan, Javier Guillermo
Xie, Hang
Brooke, Christopher B.
Yewdell, Jonathan W.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv INFLUENZA
HEMAGGLUTININ
ANTIBODY ESCAPE
VIRAL EVOLUTION
topic INFLUENZA
HEMAGGLUTININ
ANTIBODY ESCAPE
VIRAL EVOLUTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Rapid antigenic evolution enables the persistence of seasonal influenza A and B viruses in human populations despite widespread herd immunity. Understanding viral mechanisms that enable antigenic evolution is critical for designing durable vaccines and therapeutics. Here, we utilize the primerID method of error-correcting viral population sequencing to reveal an unexpected role for hemagglutinin (HA) glycosylation in compensating for fitness defects resulting from escape from anti-HA neutralizing antibodies. Antibody-free propagation following antigenic escape rapidly selected viruses with mutations that modulated receptor binding avidity through the addition of N-linked glycans to the HA globular domain. These findings expand our understanding of the viral mechanisms that maintain fitness during antigenic evolution to include glycan addition, and highlight the immense power of high-definition virus population sequencing to reveal novel viral adaptive mechanisms.
Fil: Kosik, Ivan. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Ince, William L.. National Institute of Allergy and Infectious Diseases; Estados Unidos. National Center For Toxicological Research. Food And Drug Administration; Estados Unidos
Fil: Gentles, Lauren E.. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Oler, Andrew J.. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Kosikova, Martina. National Center For Toxicological Research. Food And Drug Administration; Estados Unidos
Fil: Angel, Matthew. National Institute of Allergy and Infectious Diseases; Estados Unidos
Fil: Magadan, Javier Guillermo. National Institute of Allergy and Infectious Diseases; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Xie, Hang. National Center For Toxicological Research. Food And Drug Administration; Estados Unidos
Fil: Brooke, Christopher B.. University of Illinois at Urbana; Estados Unidos
Fil: Yewdell, Jonathan W.. National Institute of Allergy and Infectious Diseases; Estados Unidos
description Rapid antigenic evolution enables the persistence of seasonal influenza A and B viruses in human populations despite widespread herd immunity. Understanding viral mechanisms that enable antigenic evolution is critical for designing durable vaccines and therapeutics. Here, we utilize the primerID method of error-correcting viral population sequencing to reveal an unexpected role for hemagglutinin (HA) glycosylation in compensating for fitness defects resulting from escape from anti-HA neutralizing antibodies. Antibody-free propagation following antigenic escape rapidly selected viruses with mutations that modulated receptor binding avidity through the addition of N-linked glycans to the HA globular domain. These findings expand our understanding of the viral mechanisms that maintain fitness during antigenic evolution to include glycan addition, and highlight the immense power of high-definition virus population sequencing to reveal novel viral adaptive mechanisms.
publishDate 2018
dc.date.none.fl_str_mv 2018-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/91035
Kosik, Ivan; Ince, William L.; Gentles, Lauren E.; Oler, Andrew J.; Kosikova, Martina; et al.; Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs; Public Library of Science; Plos Pathogens; 14; 1; 1-2018; 1-19; e1006796
1553-7366
CONICET Digital
CONICET
url http://hdl.handle.net/11336/91035
identifier_str_mv Kosik, Ivan; Ince, William L.; Gentles, Lauren E.; Oler, Andrew J.; Kosikova, Martina; et al.; Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs; Public Library of Science; Plos Pathogens; 14; 1; 1-2018; 1-19; e1006796
1553-7366
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.ppat.1006796
info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006796
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781595725332480
score 12.928904

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