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

Thomas Spies, Vincenzo Cerundolo, Marco Colonna, Peter Cresswell, Alain Townsend, Robert DeMars

Research output: Contribution to journalArticle

288 Scopus citations

Abstract

MAJOR histocompatibility complex (MHC) class I molecules present peptides derived from the endogenous protein pool to cytotoxic T lymphocytes, which can thus recognize intracellular antigen1-3. This pathway may depend on a transporter (PSF1) (refs 4-6) to mediate entry of the cytosolic peptides into a pre-Golgi compartment where they hind to class I heavy chains and promote their stable assembly with β2-microglobulin7-12. There is, however, only indirect support for this function of PSF1 (ref. 6). 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 poly peptide is associated with a complementary transporter chain, which is polymorphic and is encoded by the PSF2 gene13, which is closely linked to PSF1.

Original languageEnglish
Pages (from-to)644-646
Number of pages3
JournalNature
Volume355
Issue number6361
DOIs
StatePublished - Jan 1 1992
Externally publishedYes

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