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Peptide motifs of closely related HLA class I molecules encompass substantial differences

Item Type:Article
Title:Peptide motifs of closely related HLA class I molecules encompass substantial differences
Creators Name:Roetzschke, O. and Falk, K. and Stevanovic, S. and Jung, G. and Rammensee, H.G.
Abstract:The peptides presented by major histocompatibility complex class I molecules adhere to strict rules concerning peptide length and occupancy by certain amino acid residues at anchor positions. Peptides presented by HLA-A*0201 molecules, for example, are generally nonapeptides requiring Leu or Met at position 2 and an aliphatic residue, predominantly Val, at position 9. A closely related molecule, HLA-A*0205, differing from the former at four amino acid residues, has a related but substantially different peptide motif. A*0205-presented peptides are still nonapeptides, and position 9 is still aliphatic, although it is preferentially occupied by Leu instead of Val. Position 2 not only allows aliphatic residues but also polar ones. Occupancy at position 6, considered as an auxiliary anchor in A*0201, as well as non-anchor residues at positions 3, 4, and 8 are relatively well conserved between the two peptide motifs. Thus, although a number of the T cell epitopes presented by the two HLA-A2 forms is expected to be identical, a considerable number of epitopes should be different.
Keywords:Amino Acid Sequence, HLA-A Antigens, Molecular Sequence Data
Source:European Journal of Immunology
Page Range:2453-2456
Date:1 September 1992
Official Publication:https://doi.org/10.1002/eji.1830220940
PubMed:View item in PubMed

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