The murine cytomegalovirus immunoevasin gp40 binds MHC class I molecules to retain them in the early secretory pathway

J Cell Sci. 2016 Jan 1;129(1):219-27. doi: 10.1242/jcs.175620. Epub 2015 Nov 2.


In the presence of the murine cytomegalovirus (mCMV) gp40 (m152) protein, murine major histocompatibility complex (MHC) class I molecules do not reach the cell surface but are retained in an early compartment of the secretory pathway. We find that gp40 does not impair the folding or high-affinity peptide binding of the class I molecules but binds to them, leading to their retention in the endoplasmic reticulum (ER), the ER-Golgi intermediate compartment (ERGIC) and the cis-Golgi, most likely by retrieval from the cis-Golgi to the ER. We identify a sequence in gp40 that is required for both its own retention in the early secretory pathway and for that of class I molecules.

Keywords: Antigen presentation; ERGIC and cis-Golgi retention; Early secretory pathway; Immune evasion; Murine cytomegalovirus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Histocompatibility Antigens Class I / metabolism*
  • Mice
  • Models, Biological
  • Muromegalovirus / metabolism*
  • Peptides / metabolism
  • Protein Binding
  • Secretory Pathway*
  • Viral Proteins / metabolism*


  • Histocompatibility Antigens Class I
  • Peptides
  • Viral Proteins