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The Molecular Basis of Allorecognition

The Molecular Basis of Allorecognition Until recently it was generally assumed that the focus of T cell receptor recognition of allogeneic MHC molecules was the polymorphic regions on the molecule that differed between responder and stimulator. It is now clear that all T cell recognition, including self-tolerance and allorecognition , involves both the MHC molecule and its associated peptide ligand. Poly­ morphic residues located within the peptide binding groove of the MHC and inaccessible to the T cell receptor can profoundly affect selection and recognition of bound peptides. These peptide differences between histoincompatible individuals greatly amplify the antigenic impact of MHC polymorphism and result in the high frequency of alloreactive cells. Evidence for the role of peptides in allorecognition is reviewed. INTRODUCTION The basis for recognition of alloantigen is one of the most historically significant issues in immunology ( 1, l a). Indeed, the identification of the targets of allograft rejection led to the definition of MHC gene products. The vigorous T cell response observed during graft rejection, and its in vitro correlate, mixed lymphocyte culture, has also been one of the most perplexing issues in immunology. In contrast to the low frequency of T cells that recognize conventional antigens, as many as http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Immunology Annual Reviews

The Molecular Basis of Allorecognition

Sherman, L A; Chattopadhyay, S
Annual Review of Immunology , Volume 11 (1) – Apr 1, 1993
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Publisher
Annual Reviews
Copyright
Copyright 1993 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0732-0582
eISSN
1545-3278
DOI
10.1146/annurev.iy.11.040193.002125
pmid
8476567
Publisher site
See Article on Publisher Site

Abstract

Until recently it was generally assumed that the focus of T cell receptor recognition of allogeneic MHC molecules was the polymorphic regions on the molecule that differed between responder and stimulator. It is now clear that all T cell recognition, including self-tolerance and allorecognition , involves both the MHC molecule and its associated peptide ligand. Poly­ morphic residues located within the peptide binding groove of the MHC and inaccessible to the T cell receptor can profoundly affect selection and recognition of bound peptides. These peptide differences between histoincompatible individuals greatly amplify the antigenic impact of MHC polymorphism and result in the high frequency of alloreactive cells. Evidence for the role of peptides in allorecognition is reviewed. INTRODUCTION The basis for recognition of alloantigen is one of the most historically significant issues in immunology ( 1, l a). Indeed, the identification of the targets of allograft rejection led to the definition of MHC gene products. The vigorous T cell response observed during graft rejection, and its in vitro correlate, mixed lymphocyte culture, has also been one of the most perplexing issues in immunology. In contrast to the low frequency of T cells that recognize conventional antigens, as many as

Journal

Annual Review of Immunology – Annual Reviews

Published: Apr 1, 1993

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