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A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

PeaceBrewer, AL, Tussey, LG, Matsui, M, Li, GX, Quinn, Daniel and Frelinger, JA (1996) A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. IMMUNITY, 4 (5). pp. 505-514. [Journal article]

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DOI: 10.1016/S1074-7613(00)80416-1

Abstract

Mutating the HLA-A*0201 heavy chain from threonine to lysine at position 134 (T134K) results in a molecule that presents exogenous peptide, but cannot present endogenously derived antigen. This is reflected in diminished cell surface expression and altered intracellular trafficking of T134K. The failure of T134K to present endogenous antigen can be overcome by using an ER targeting sequence, suggesting that the antigen presentation defect is restricted to TAP-dependent peptide loading. The ability of T134K to load peptide in a TAP-dependent manner is dramatically reduced compared with HLA-A*0201. By coimmunoprecipitation there is no detectable association of the T134K molecule with the TAP complex. Thus, T134K selectively affects TAP association and peptide loading, suggesting a requirement for the direct interaction of MHC class I heavy chain and the TAP complex for efficient presentation of endogenous antigen.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
ID Code:22902
Deposited By:Dr Daniel Quinn
Deposited On:31 Jul 2012 10:28
Last Modified:31 Jul 2012 10:28

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