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Major histocompatibility complex (MHC) class I molecules present peptides derived from the endogenous protein pool to cytotoxic T lymphocytes, which can thus recognize intracellular antigen. This pathway may depend on a transporter (PSF1) to mediate entry of the cytosolic peptides into a pre-Golgi compartment where they bind to class I heavy chains and promote their stable assembly with beta 2-microglobulin. There is, however, only indirect support for this function of PSF1. Here we show that PSF1 is necessary for the efficient assembly of class I molecules and enables them to present a peptide epitope derived from endogenously synthesized viral antigen. Immunochemical and genetic data demonstrate that the PSF1 polypeptide is associated with a complementary transporter chain, which is polymorphic and is encoded by the PSF2 gene, which is closely linked to PSF1.

Original publication

DOI

10.1038/355644a0

Type

Journal article

Journal

Nature

Publication Date

13/02/1992

Volume

355

Pages

644 - 646

Keywords

Antigens, Viral, Base Sequence, Electrophoresis, Polyacrylamide Gel, HLA-A2 Antigen, Histocompatibility Antigens Class I, Humans, In Vitro Techniques, Influenza A virus, Molecular Sequence Data, T-Lymphocytes, Cytotoxic, Transfection