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The luminal part of the murine cytomegalovirus glycoprotein gp40 catalyzes the retention of MHC class I molecules
Author(s) -
Ziegler Heike,
Muranyi Walter,
Burgert HansGerhard,
Kremmer Elisabeth,
Koszinowski Ulrich H.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.5.870
Subject(s) - biology , mhc class i , transporter associated with antigen processing , golgi apparatus , major histocompatibility complex , microbiology and biotechnology , endosome , cd74 , mhc restriction , antigen processing , transmembrane protein , endoplasmic reticulum , antigen presentation , secretory pathway , biochemistry , antigen , genetics , t cell , immune system , receptor , intracellular
Murine cytomegalovirus (MCMV) interferes with the MHC class I pathway of antigen presentation. The type I transmembrane glycoprotein gp40, encoded by the gene m152 , retains major histocompatibility complex (MHC) class I complexes in the endoplasmic reticulum (ER)–Golgi intermediate compartment (ERGIC)/ cis ‐Golgi. These MHC class I complexes are stable, show an extended half‐life and do not exchange β 2 ‐microglobulin, whereas gp40 reaches an endosomal/lysosomal compartment where it subsequently is degraded. The analysis of regions within the viral protein that are essential for MHC class I retention revealed that a secreted form of gp40, lacking the cytoplasmic tail and the transmembrane region, still has the capacity to retain MHC class I complexes. Continuous expression of gp40 is not required for MHC class I retention. Our data indicate that the retention of MHC class I complexes in the ERGIC/ cis ‐Golgi is triggered by gp40 and does not require the further presence of the viral protein.