A common minimal motif for the ligands of HLA-B*27 class I molecules

CD8(+) T cells identify and kill infected cells through the specific recognition of short viral antigens bound to human major histocompatibility complex (HLA) class I molecules. The colossal number of polymorphisms in HLA molecules makes it essential to characterize the antigen-presenting properties...

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Detalles Bibliográficos
Autores: Barriga, Alejandro, Lorente, Elena, Johnstone, Carolina, Mir-Gerrero, Carmen, Val, Margarita del, Lopez, Daniel
Tipo de recurso: artículo
Fecha de publicación:2014
País:España
Institución:Instituto de Salud Carlos III (ISCIII)
Repositorio:Repisalud
Idioma:inglés
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/6886
Acceso en línea:http://hdl.handle.net/20.500.12105/6886
Access Level:acceso abierto
Palabra clave:Amino Acid Motifs
Animals
Antigen Presentation
Antigens, Viral, Tumor
Cell Line
HLA-B27 Antigen
Humans
Ligands
Mice
Protein Binding
Protein Stability
Respiratory Syncytial Virus, Human
Viral Proteins
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repository_id_str
spelling A common minimal motif for the ligands of HLA-B*27 class I moleculesBarriga, AlejandroLorente, ElenaJohnstone, CarolinaMir-Gerrero, CarmenVal, Margarita delLopez, DanielAmino Acid MotifsAnimalsAntigen PresentationAntigens, Viral, TumorCell LineHLA-B27 AntigenHumansLigandsMiceProtein BindingProtein StabilityRespiratory Syncytial Virus, HumanViral ProteinsCD8(+) T cells identify and kill infected cells through the specific recognition of short viral antigens bound to human major histocompatibility complex (HLA) class I molecules. The colossal number of polymorphisms in HLA molecules makes it essential to characterize the antigen-presenting properties common to large HLA families or supertypes. In this context, the HLA-B*27 family comprising at least 100 different alleles, some of them widely distributed in the human population, is involved in the cellular immune response against pathogens and also associated to autoimmune spondyloarthritis being thus a relevant target of study. To this end, HLA binding assays performed using nine HLA-B*2705-restricted ligands endogenously processed and presented in virus-infected cells revealed a common minimal peptide motif for efficient binding to the HLA-B*27 family. The motif was independently confirmed using four unrelated peptides. This experimental approach, which could be easily transferred to other HLA class I families and supertypes, has implications for the validation of new bioinformatics tools in the functional clustering of HLA molecules, for the identification of antiviral cytotoxic T lymphocyte responses, and for future vaccine development.Public Library of Science (PLOS)Ministerio de Economía y Competitividad (España)20182018-12-1820142014-09-0120142014-09-01research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/20.500.12105/6886reponame:Repisaludinstname:Instituto de Salud Carlos III (ISCIII)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 4.0 Internacionalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repisalud.isciii.es:20.500.12105/68862026-06-12T12:43:37Z
dc.title.none.fl_str_mv A common minimal motif for the ligands of HLA-B*27 class I molecules
title A common minimal motif for the ligands of HLA-B*27 class I molecules
spellingShingle A common minimal motif for the ligands of HLA-B*27 class I molecules
Barriga, Alejandro
Amino Acid Motifs
Animals
Antigen Presentation
Antigens, Viral, Tumor
Cell Line
HLA-B27 Antigen
Humans
Ligands
Mice
Protein Binding
Protein Stability
Respiratory Syncytial Virus, Human
Viral Proteins
title_short A common minimal motif for the ligands of HLA-B*27 class I molecules
title_full A common minimal motif for the ligands of HLA-B*27 class I molecules
title_fullStr A common minimal motif for the ligands of HLA-B*27 class I molecules
title_full_unstemmed A common minimal motif for the ligands of HLA-B*27 class I molecules
title_sort A common minimal motif for the ligands of HLA-B*27 class I molecules
dc.creator.none.fl_str_mv Barriga, Alejandro
Lorente, Elena
Johnstone, Carolina
Mir-Gerrero, Carmen
Val, Margarita del
Lopez, Daniel
author Barriga, Alejandro
author_facet Barriga, Alejandro
Lorente, Elena
Johnstone, Carolina
Mir-Gerrero, Carmen
Val, Margarita del
Lopez, Daniel
author_role author
author2 Lorente, Elena
Johnstone, Carolina
Mir-Gerrero, Carmen
Val, Margarita del
Lopez, Daniel
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)

dc.subject.none.fl_str_mv Amino Acid Motifs
Animals
Antigen Presentation
Antigens, Viral, Tumor
Cell Line
HLA-B27 Antigen
Humans
Ligands
Mice
Protein Binding
Protein Stability
Respiratory Syncytial Virus, Human
Viral Proteins
topic Amino Acid Motifs
Animals
Antigen Presentation
Antigens, Viral, Tumor
Cell Line
HLA-B27 Antigen
Humans
Ligands
Mice
Protein Binding
Protein Stability
Respiratory Syncytial Virus, Human
Viral Proteins
description CD8(+) T cells identify and kill infected cells through the specific recognition of short viral antigens bound to human major histocompatibility complex (HLA) class I molecules. The colossal number of polymorphisms in HLA molecules makes it essential to characterize the antigen-presenting properties common to large HLA families or supertypes. In this context, the HLA-B*27 family comprising at least 100 different alleles, some of them widely distributed in the human population, is involved in the cellular immune response against pathogens and also associated to autoimmune spondyloarthritis being thus a relevant target of study. To this end, HLA binding assays performed using nine HLA-B*2705-restricted ligands endogenously processed and presented in virus-infected cells revealed a common minimal peptide motif for efficient binding to the HLA-B*27 family. The motif was independently confirmed using four unrelated peptides. This experimental approach, which could be easily transferred to other HLA class I families and supertypes, has implications for the validation of new bioinformatics tools in the functional clustering of HLA molecules, for the identification of antiviral cytotoxic T lymphocyte responses, and for future vaccine development.
publishDate 2014
dc.date.none.fl_str_mv 2014
2014-09-01
2014
2014-09-01
2018
2018-12-18
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12105/6886
url http://hdl.handle.net/20.500.12105/6886
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Public Library of Science (PLOS)
publisher.none.fl_str_mv Public Library of Science (PLOS)
dc.source.none.fl_str_mv reponame:Repisalud
instname:Instituto de Salud Carlos III (ISCIII)
instname_str Instituto de Salud Carlos III (ISCIII)
reponame_str Repisalud
collection Repisalud
repository.name.fl_str_mv
repository.mail.fl_str_mv
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