Presentation of three different viral peptides is determined by common structural features of the human lymphocyte antigen-A2.1 molecule.

Important note: Information in this article was accurate in 1993. The state of the art may have changed since the publication date.

Presentation of three different viral peptides is determined by common structural features of the human lymphocyte antigen-A2.1 molecule.

J Immunother. 1992 Oct;12(3):180-2. Unique Identifier : AIDSLINE MED/93075652
Utz U; Biddison WE; Molecular Immunology Section, National Institute of Neurological; Disorders and Stroke, National Institutes of Health, Bethesda, MD; 20892.

Abstract: To assess whether similar or dissimilar molecular features of class I human lymphocyte antigen (HLA) molecules determine the presentation of structurally diverse peptides, we have examined the influence of different pockets within the HLA-A2.1 molecule on the presentation of three different viral peptides. The influenza virus M1 58-66, HTLV-I Tax peptide 12-19, and HCMV gB 619-628 are minimal peptides that induce HLA-A2.1-restricted non-cross-reactive CTL responses. The influence of distinct structural features of HLA-A2.1 on peptide presentation was analyzed using a panel of 14 HLA-A2 mutants each with single amino acid substitutions in one of six pockets that are located in the peptide binding site. Ten of the 14 mutants showed concordant effects on the presentation of all three peptides to their peptide-specific CTL lines. Four of the mutants had a negative effect on the presentation of only one or two of these viral peptides. These findings indicate that common structural features in HLA-A2 determine the binding and conformation of different peptides, and help to provide a plausible explanation for how diverse peptides bind to HLA-A2.

Keywords: Amino Acid Sequence Binding Sites Human HLA-A2 Antigen/CHEMISTRY/GENETICS/*IMMUNOLOGY HTLV-I/IMMUNOLOGY Models, Molecular Molecular Sequence Data Orthomyxoviridae/IMMUNOLOGY Peptides/CHEMISTRY/*IMMUNOLOGY T-Lymphocytes, Cytotoxic/*IMMUNOLOGY JOURNAL ARTICLE
930330
M9331079

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