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Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope
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Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope
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Journal Article
Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope
2017
Overview
Crystal structure analysis combined with sequencing approaches uncover a broad T cell receptor repertoire and reveal the structural basis of influenza M1 epitope recognition.
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.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Animals
/ Antigens
/ CD8-Positive T-Lymphocytes - metabolism
/ Cells
/ Complementarity Determining Regions - chemistry
/ Epitopes
/ Epitopes, T-Lymphocyte - chemistry
/ Epitopes, T-Lymphocyte - metabolism
/ Histocompatibility antigen HLA
/ Humans
/ Immunodominant Epitopes - chemistry
/ Immunodominant Epitopes - metabolism
/ Major Histocompatibility Complex
/ Peptides
/ Protein Structure, Secondary
/ Receptors, Antigen, T-Cell - chemistry
/ Receptors, Antigen, T-Cell - genetics
