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Alloreactive cytotoxic T-lymphocyte-defined HLA-B7 subtypes differ in peptide antigen presentation.
- Source :
-
Immunogenetics [Immunogenetics] 1996; Vol. 43 (1-2), pp. 27-37. - Publication Year :
- 1996
-
Abstract
- We investigated T-cell-defined HLA-B7 subtypes using cDNA sequencing, analysis of bound peptides, and reactivity with a panel of alloreactive cytotoxic T-lymphocyte (CTL) clones. Three subtypes (HLA-B*0702, HLA-B*0703, and HLA-B*0705) differ in nucleotide and predicted amino acid sequence. CTL reactivity and pooled peptide sequencing show that these three HLA-B7 subtypes bind distinct but overlapping sets of peptides. In particular B*0702 expresses D pocket residue Asp 114 and binds peptides with P3 Arg, whereas B*0705 expresses D pocket residue Asn 114 and binds peptides with P3 Ala, Leu, and Met. Consistent with different peptide-binding specificities, three alloreactive CTL differentiate between cells expressing B*0702, B*0703, and B*0705 by detecting specific peptide/HLA-B7 complexes. In contrast, three other T-cell-defined HLA-B7 subtypes are identical to HLA-B*0702. The B*0702-expressing cell lines are differentiated by two of ten CTL clones. One CTL clone differentiates B*0702-expressing cells by their ability to present peptide antigen. Thus differences in peptide presentation can explain differential CTL recognition of cell lines expressing structurally identical and variant HLA-B7.
- Subjects :
- Amino Acid Sequence
Base Sequence
CD58 Antigens biosynthesis
DNA, Complementary genetics
HLA-B7 Antigen biosynthesis
HLA-B7 Antigen chemistry
HLA-B7 Antigen classification
HLA-B7 Antigen genetics
Intercellular Adhesion Molecule-1 biosynthesis
Molecular Sequence Data
Protein Conformation
Sequence Alignment
Antigen Presentation
Genes, MHC Class I
HLA-B7 Antigen immunology
Peptide Fragments immunology
T-Lymphocytes, Cytotoxic immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0093-7711
- Volume :
- 43
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Immunogenetics
- Publication Type :
- Academic Journal
- Accession number :
- 8537119
- Full Text :
- https://doi.org/10.1007/BF00186601