Peptides naturally presented by MHC class I molecules

Item Type:	Review
Title:	Peptides naturally presented by MHC class I molecules
Creators Name:	Rammensee, H.G. and Falk, K. and Roetzschke, O.
Abstract:	MHC class I molecules are peptide receptors of stringent specificity which however still allow millions of different ligands. This is achieved by the following specificity characteristics summarized as allele specific peptide motifs: Peptides are of defined length, depending on the class I allele (either 8 or 9 residues; exceptions have been observed). Typically, 2 of the 8 or 9 positions are anchors that can only be occupied by a single amino acid residue, or by residues with closely related side chains. Location and characteristics of anchors vary with class I alleles. The C terminus of the peptide ligands is frequently an aliphatic or charged residue. Such allele-specific class I peptide ligand motifs, known so far for H-2Kd, Kb, Kk, Kkm1, Db, HLA-A0201, A0205, and B*2705, are useful to predict natural T cell epitopes. The latter can be determined by extraction from cells recognized by the T cell of interest. It is not known how the class I ligands are produced in the cell, although speculative models exist. The peptide specificity of class I molecules and experimental evidence indicate that T cells are tolerant to only a small fraction of the expressed genomic sequences and are not tolerant to the remainder. The function of class I molecules is to present a collection of self-peptide samples at the cell surface for surveillance by T cells.
Keywords:	MHC Class I, Antigen Processing, Antigen Presentation, Peptide Motifs, T Lymphocytes, Animals, Mice
Source:	Annual Review of Immunology
ISSN:	0732-0582
Publisher:	Annual Reviews
Volume:	11
Page Range:	213-244
Date:	1 January 1993
Official Publication:	https://doi.org/10.1146/annurev.iy.11.040193.001241
PubMed:	View item in PubMed

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