Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer

Nature. 1992 Feb 13;355(6361):644-6. doi: 10.1038/355644a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

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


  • Antigens, Viral
  • HLA-A2 Antigen
  • Histocompatibility Antigens Class I