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dc.contributor.authorSong, InYoung
dc.contributor.authorGil, Anna
dc.contributor.authorMishra, Rabinarayan
dc.contributor.authorGhersi, Dario
dc.contributor.authorSelin, Liisa K.
dc.contributor.authorStern, Lawrence J.
dc.date2022-08-11T08:09:47.000
dc.date.accessioned2022-08-23T16:43:40Z
dc.date.available2022-08-23T16:43:40Z
dc.date.issued2017-04-01
dc.date.submitted2017-09-21
dc.identifier.citation<p>Nat Struct Mol Biol. 2017 Apr;24(4):395-406. doi: 10.1038/nsmb.3383. Epub 2017 Feb 27. <a href="https://doi.org/10.1038/nsmb.3383">Link to article on publisher's site</a></p>
dc.identifier.issn1545-9985 (Linking)
dc.identifier.doi10.1038/nsmb.3383
dc.identifier.pmid28250417
dc.identifier.urihttp://hdl.handle.net/20.500.14038/40343
dc.description<p>First author InYoung Song is a doctoral student in the Immunology and Microbiology program in the Graduate School of Biomedical Sciences (GSBS) at UMass Medical School.</p>
dc.description.abstractA keystone of antiviral immunity is CD8+ T cell recognition of viral peptides bound to MHC-I proteins. The recognition modes of individual T cell receptors (TCRs) have been studied in some detail, but the role of TCR variation in providing a robust response to viral antigens is unclear. The influenza M1 epitope is an immunodominant target of CD8+ T cells that help to control influenza in HLA-A2+ individuals. Here we show that CD8+ T cells use many distinct TCRs to recognize HLA-A2-M1, which enables the use of different structural solutions to the problem of specifically recognizing a relatively featureless peptide antigen. The vast majority of responding TCRs target a small cleft between HLA-A2 and the bound M1 peptide. These broad repertoires lead to plasticity in antigen recognition and protection against T cell clonal loss and viral escape.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=28250417&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5383516/
dc.subjectUMCCTS funding
dc.subjectBiochemistry
dc.subjectImmunology and Infectious Disease
dc.subjectImmunopathology
dc.subjectMolecular Biology
dc.subjectStructural Biology
dc.titleBroad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope
dc.typeJournal Article
dc.source.journaltitleNature structural and molecular biology
dc.source.volume24
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/3142
dc.identifier.contextkey10782030
html.description.abstract<p>A keystone of antiviral immunity is CD8+ T cell recognition of viral peptides bound to MHC-I proteins. The recognition modes of individual T cell receptors (TCRs) have been studied in some detail, but the role of TCR variation in providing a robust response to viral antigens is unclear. The influenza M1 epitope is an immunodominant target of CD8+ T cells that help to control influenza in HLA-A2+ individuals. Here we show that CD8+ T cells use many distinct TCRs to recognize HLA-A2-M1, which enables the use of different structural solutions to the problem of specifically recognizing a relatively featureless peptide antigen. The vast majority of responding TCRs target a small cleft between HLA-A2 and the bound M1 peptide. These broad repertoires lead to plasticity in antigen recognition and protection against T cell clonal loss and viral escape.</p>
dc.identifier.submissionpathoapubs/3142
dc.contributor.departmentGraduate School of Biomedical Sciences, Immunology and Microbiology Program
dc.contributor.departmentDepartment of Pathology
dc.source.pages395-406


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