Control of MHC class I traffic from the endoplasmic reticulum by cellular chaperones and viral anti-chaperones

Albrecht Gruhler, Klaus Früh

Research output: Contribution to journalArticle

19 Scopus citations


MHC class I molecules assemble with peptides in the endoplasmic reticulum (ER). To ensure that only peptide-loaded MHC molecules leave the ER, empty molecules are retained by ER-resident chaperones, most notably the MHC-specific tapasin. ER exit of class I MHC is also controlled by viruses, but for the opposite purpose of preventing peptide presentation to T cells. Interestingly, some viral proteins are able to retain MHC class I molecules in the ER despite being transported. By contrast, other viral proteins exit the ER only upon binding to class I MHC, thereby rerouting newly synthesized class I molecules to intracellular sites of proteolysis. Thus, immune escape can be achieved by reversing, inhibiting or redirecting the chaperone-assisted MHC class I folding, assembly and intracellular transport.

Original languageEnglish (US)
Pages (from-to)306-311
Number of pages6
Issue number4
StatePublished - Jan 1 2000



  • Antigen presentation
  • Endoplasmic reticulum
  • Golgi
  • Histocompatability complex
  • Immune escape
  • Intracellular protein transport

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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