Abstract
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 language | English (US) |
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Pages (from-to) | 306-311 |
Number of pages | 6 |
Journal | Traffic |
Volume | 1 |
Issue number | 4 |
DOIs | |
State | Published - 2000 |
Externally published | Yes |
Keywords
- Antigen presentation
- Endoplasmic reticulum
- Golgi
- Histocompatability complex
- Immune escape
- Intracellular protein transport
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology