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The Structure of T-Cell Epitopes

The Structure of T-Cell Epitopes The humoral and cellular arms of the adaptive immune response, mediated by B and T lymphocytes respectively, differ fundamentally in the way in which they recognize antigen. The B-cell receptor for antigen (immuno­ globulin) can bind to soluble antigen in a manner similar to that of many well-characterized receptor-ligand systems. In contrast, the T-cell antigen receptor can generally recognize antigen only in association with cell surface molecules encoded by the major histocompatibility complex (MHC). This requirement, known as MHC restriction, ensures that T­ cell activation or effector function occurs only i n an appropriate cellular context. Antigen-specific T-cell activation thus results from the formation of a ternary complex involving the T-cell receptor (TcR), nominal antigen, and class-l or class-II MHC molecules (1, 2). Characterization of the antigen-specific receptors on T-helper and cyto­ toxic cells unfortunately did not suggest any structural b asis for the MHC­ restricted recognition of antigen. On the contrary, the genes encoding the oc and f3 chains of the TcR heterodimer showed marked homology with immunoglobulin genes, and similar mechanisms of DNA rearrangement appeared to be involved in the generation of both T- and B-cell repertoires (3-5). Experiments to determine the mechanism underlying MHC restric­ http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Immunology Annual Reviews

The Structure of T-Cell Epitopes

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Publisher
Annual Reviews
Copyright
Copyright 1987 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0732-0582
eISSN
1545-3278
DOI
10.1146/annurev.iy.05.040187.002401
pmid
2439104
Publisher site
See Article on Publisher Site

Abstract

The humoral and cellular arms of the adaptive immune response, mediated by B and T lymphocytes respectively, differ fundamentally in the way in which they recognize antigen. The B-cell receptor for antigen (immuno­ globulin) can bind to soluble antigen in a manner similar to that of many well-characterized receptor-ligand systems. In contrast, the T-cell antigen receptor can generally recognize antigen only in association with cell surface molecules encoded by the major histocompatibility complex (MHC). This requirement, known as MHC restriction, ensures that T­ cell activation or effector function occurs only i n an appropriate cellular context. Antigen-specific T-cell activation thus results from the formation of a ternary complex involving the T-cell receptor (TcR), nominal antigen, and class-l or class-II MHC molecules (1, 2). Characterization of the antigen-specific receptors on T-helper and cyto­ toxic cells unfortunately did not suggest any structural b asis for the MHC­ restricted recognition of antigen. On the contrary, the genes encoding the oc and f3 chains of the TcR heterodimer showed marked homology with immunoglobulin genes, and similar mechanisms of DNA rearrangement appeared to be involved in the generation of both T- and B-cell repertoires (3-5). Experiments to determine the mechanism underlying MHC restric­

Journal

Annual Review of Immunology – Annual Reviews

Published: Apr 1, 1987

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