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Binding of nonamer peptides to three HLA-B51 molecules which differ by a single amino acid substitution in the A-pocket.
- Source :
- Immunogenetics; 1996, Vol. 43 Issue 5, p268-276, 9p
- Publication Year :
- 1996
-
Abstract
- The interaction between 9-mer peptides and HLA-B51 molecules was investigated by quantitative peptide binding assay using RMA-S cell expressing human β2-microglobulin and HLA-B51 molecules. Of 147 chemically synthesized 9-mer peptides possessing two anchor residues corresponding to the motif of HLA-B5101 binding self-peptides, 27 paptides bound to HLA-B5101 molecules. Pro and Ala at position 2 as well as Ile at position 9 were confirmed to be main anchor residues, while Gly at position 2 as well as Val, Leu, and Met at position 9 were weak anchor residues for HLA-B5101. The A-pocket is suspected to have a critical role in peptide binding to MHC class I molecules because this pocket corresponds to the N-terminus of peptides and has a strong hydrogen bond formed by conserved Tyr residues. Further analysis of peptide binding to HLA-B5102 and B5103 molecules showed that a single amino acid substitution of Tyor for His at residue 171(B5102) and that of Gly for Trp at residue 167 (B5103) has a minimum effect in HLA-B51-peptide binding. Since previous studies showed that some HLA-B51 alloreactive CTL clones failed to kill the cells expressing HLA-B5102 or HLA-B5103, these results imply that the structural change of the A-pocket among HLA-B51 subtypes causes a critical conformational change of the epitope for TCR recognition rather than influences the interaction between peptides and MHC class I molecules. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00937711
- Volume :
- 43
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Immunogenetics
- Publication Type :
- Academic Journal
- Accession number :
- 70620500
- Full Text :
- https://doi.org/10.1007/BF02440994