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Tapasin is a 48-kDa endoplasmic reticulum (ER)-resident glycoprotein that binds to the transporter associated with antigen processing (TAP) and mediates an interaction between TAP and newly synthesized MHC class I molecules. It is also essential for the proper antigen presenting function of HLA-A*0101 (HLA-A1), HLA-A*0801 (HLA-B8) and HLA-B*4402 (HLA-B4402). We show here that while tapasin is required for HLA-A*0201 (HLA-A2) molecules to bind to TAP, its absence does not block the presentation of HLA-A2-restricted TAP-dependent epitopes to cytotoxic T lymphocytes indicating that, unlike HLA-A1, HLA-B8 and HLA-B4402, HLA-A2 has access to the TAP-dependent peptide pool even in the absence of tapasin. Nevertheless, the overall efficiency with which HLA-A2 was loaded with optimal, stabilizing peptides was impaired in the cell line .220, resulting in a significant increase in the fraction of HLA-A2 molecules being released from the ER in a "peptide-receptive" state.

Original publication

DOI

10.1002/(sici)1521-4141(199810)28:10<3214::aid-immu3214>3.0.co;2-c

Type

Journal article

Journal

European journal of immunology

Publication Date

10/1998

Volume

28

Pages

3214 - 3220

Addresses

Nuffield Department of Clinical Medicine, University of Oxford, John Radcliffe Hospital, GB.

Keywords

T-Lymphocytes, Cytotoxic, Cell Line, Humans, Peptides, Immunoglobulins, Membrane Transport Proteins, Antiporters, HLA-A2 Antigen, Epitopes, T-Lymphocyte, Antigen Presentation