T cell antigen receptor recognition of antigen-presenting molecules

Jamie Rossjohn, Stephanie Gras, John J Miles, Stephen J Turner, Dale I Godfrey, James McCluskey

Research output: Contribution to journalArticleResearchpeer-review

Abstract

The Major Histocompatibility Complex (MHC) locus encodes classical MHC class I andMHCclass II molecules and nonclassical MHC-I molecules. The architecture of these molecules is ideally suited to capture and present an array of peptide antigens (Ags). In addition, the CD1 family members and MR1 are MHC class I?like molecules that bind lipid-based Ags and vitamin B precursors, respectively. These Ag-bound molecules are subsequently recognized by T cell antigen receptors (TCRs) expressed on the surface of Tlymphocytes. Structural and associated functional studies have been highly informative in providing insight into these interactions, which are crucial to immunity, and how they can lead to aberrant T cell reactivity. Investigators have determined over thirty unique TCR-peptide-MHC-I complex structures and twenty unique TCR-peptide-MHC-II complex structures. These investigations have shown a broad consensus in docking geometry andprovided insight into MHC restriction. Structural studies on TCR-mediated recognition of lipid and metabolite Ags have been mostly confined to TCRs from innate-like natural killer T cells and mucosal-associated invariant T cells, respectively. These studies revealed clear differences between TCR-lipid-CD1, TCR-metabolite-MR1, and TCR-peptide-MHC recognition. Accordingly, TCRs show remarkable structural and biological versatility in engaging different classes of Ag that are presented by polymorphic and monomorphic Ag-presenting molecules of the immune system.
Original languageEnglish
Pages (from-to)169 - 200
Number of pages32
JournalAnnual Review of Immunology
Volume33
DOIs
Publication statusPublished - 2015

Cite this

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title = "T cell antigen receptor recognition of antigen-presenting molecules",
abstract = "The Major Histocompatibility Complex (MHC) locus encodes classical MHC class I andMHCclass II molecules and nonclassical MHC-I molecules. The architecture of these molecules is ideally suited to capture and present an array of peptide antigens (Ags). In addition, the CD1 family members and MR1 are MHC class I?like molecules that bind lipid-based Ags and vitamin B precursors, respectively. These Ag-bound molecules are subsequently recognized by T cell antigen receptors (TCRs) expressed on the surface of Tlymphocytes. Structural and associated functional studies have been highly informative in providing insight into these interactions, which are crucial to immunity, and how they can lead to aberrant T cell reactivity. Investigators have determined over thirty unique TCR-peptide-MHC-I complex structures and twenty unique TCR-peptide-MHC-II complex structures. These investigations have shown a broad consensus in docking geometry andprovided insight into MHC restriction. Structural studies on TCR-mediated recognition of lipid and metabolite Ags have been mostly confined to TCRs from innate-like natural killer T cells and mucosal-associated invariant T cells, respectively. These studies revealed clear differences between TCR-lipid-CD1, TCR-metabolite-MR1, and TCR-peptide-MHC recognition. Accordingly, TCRs show remarkable structural and biological versatility in engaging different classes of Ag that are presented by polymorphic and monomorphic Ag-presenting molecules of the immune system.",
author = "Jamie Rossjohn and Stephanie Gras and Miles, {John J} and Turner, {Stephen J} and Godfrey, {Dale I} and James McCluskey",
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language = "English",
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pages = "169 -- 200",
journal = "Annual Review of Immunology",
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T cell antigen receptor recognition of antigen-presenting molecules. / Rossjohn, Jamie; Gras, Stephanie; Miles, John J; Turner, Stephen J; Godfrey, Dale I; McCluskey, James.

In: Annual Review of Immunology, Vol. 33, 2015, p. 169 - 200.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

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AU - Gras, Stephanie

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AU - Godfrey, Dale I

AU - McCluskey, James

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AB - The Major Histocompatibility Complex (MHC) locus encodes classical MHC class I andMHCclass II molecules and nonclassical MHC-I molecules. The architecture of these molecules is ideally suited to capture and present an array of peptide antigens (Ags). In addition, the CD1 family members and MR1 are MHC class I?like molecules that bind lipid-based Ags and vitamin B precursors, respectively. These Ag-bound molecules are subsequently recognized by T cell antigen receptors (TCRs) expressed on the surface of Tlymphocytes. Structural and associated functional studies have been highly informative in providing insight into these interactions, which are crucial to immunity, and how they can lead to aberrant T cell reactivity. Investigators have determined over thirty unique TCR-peptide-MHC-I complex structures and twenty unique TCR-peptide-MHC-II complex structures. These investigations have shown a broad consensus in docking geometry andprovided insight into MHC restriction. Structural studies on TCR-mediated recognition of lipid and metabolite Ags have been mostly confined to TCRs from innate-like natural killer T cells and mucosal-associated invariant T cells, respectively. These studies revealed clear differences between TCR-lipid-CD1, TCR-metabolite-MR1, and TCR-peptide-MHC recognition. Accordingly, TCRs show remarkable structural and biological versatility in engaging different classes of Ag that are presented by polymorphic and monomorphic Ag-presenting molecules of the immune system.

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