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...
| Autores: | , , , , , |
|---|---|
| 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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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 |
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Repisalud |
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|
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1869407742488215552 |
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15,811543 |