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...
| Authors: | ; ; ; ; ; |
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| Format: | Article |
| Publication date: | 2014 |
| Country: | España |
| Institution: | Instituto de Salud Carlos III (ISCIII) |
| Repository: | Repisalud |
| Language: | English |
| OAI Identifier: | oai:repisalud.isciii.es:20.500.12105/6886 |
| Online Access: | http://hdl.handle.net/20.500.12105/6886 |
| Access Level: | Open access |
| Keyword: | 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 |
| _version_ | 1878733006336688128 |
|---|---|
| author | Barriga, Alejandro |
| author2 | Lorente, Elena Johnstone, Carolina Mir-Gerrero, Carmen Val, Margarita del Lopez, Daniel |
| author2_role | author author author author author |
| author_browse | Barriga, Alejandro Johnstone, Carolina Lopez, Daniel Lorente, Elena Mir-Gerrero, Carmen Val, Margarita del |
| author_facet | Barriga, Alejandro Lorente, Elena Johnstone, Carolina Mir-Gerrero, Carmen Val, Margarita del Lopez, Daniel |
| author_role | author |
| collection | Repisalud |
| 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. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | ES_4e39e020e22dc475120ef1bc4a2367ce |
| institution | Instituto de Salud Carlos III (ISCIII) |
| instname_str | Instituto de Salud Carlos III (ISCIII) |
| language | eng |
| network_acronym_str | ES |
| network_name_str | España |
| oai_identifier_str | oai:repisalud.isciii.es:20.500.12105/6886 |
| publishDate | 2014 |
| publishDateSort | 2014 |
| publisher | Public Library of Science (PLOS) |
| publisherStr | Public Library of Science (PLOS) |
| reponame_str | Repisalud |
| spelling | A common minimal motif for the ligands of HLA-B*27 class I molecules Barriga, Alejandro Lorente, Elena Johnstone, Carolina Mir-Gerrero, Carmen Val, Margarita del Lopez, Daniel 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 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. Public Library of Science (PLOS) http://hdl.handle.net/20.500.12105/6886 |
| 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 | 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_short | 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 |
| 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 |
| topic_facet | 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 |
| url | http://hdl.handle.net/20.500.12105/6886 |