HLA class I polymorphism has a dual impact on ligand binding and chaperone interaction

This article will describe coordinated analyses of how amino acid substitutions in the HLA class I antigen binding groove modify chaperone interaction and peptide ligand presentation. By parallel testing of ligand presentation and chaperone interaction with a series of natural HLA-B subtypes, this s...

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Bibliographic Details
Published in:Human immunology 2002-04, Vol.63 (4), p.248-255
Main Authors: Hildebrand, William H, Turnquist, Heth R, Prilliman, Kiley R, Hickman, Heather D, Schenk, Erin L, McIlhaney, Mary M, Solheim, Joyce C
Format: Article
Language:English
Subjects:
chaperones
histocompatibility antigen HLA
Histocompatibility Antigens Class I - immunology
HLA-B Antigens - genetics
HLA-B Antigens - immunology
HLA-B15 Antigen
Humans
Ligands
Molecular Chaperones - immunology
Peptides - immunology
Polymorphism, Genetic
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Summary:This article will describe coordinated analyses of how amino acid substitutions in the HLA class I antigen binding groove modify chaperone interaction and peptide ligand presentation. By parallel testing of ligand presentation and chaperone interaction with a series of natural HLA-B subtypes, this study has discovered that position 116 of the HLA-B15 class I heavy chain is pivotal in both peptide selection and control of interaction between the assembly complex and the class I heavy chain. Correlated with these qualitative differences in peptide selection and chaperone association are quantitative differences in the expression levels of the HLA molecules at the cell surface. These parallel studies, therefore, demonstrate that particular HLA class I polymorphisms can simultaneously influence ligand presentation and interaction with intracellular chaperones.
ISSN:0198-8859
DOI:10.1016/S0198-8859(02)00364-6