Abstract
Qa-1b and its human homolog, HLA-E, predominantly bind leader peptides derived from other class I molecules. Their presentation is TAP-dependent and proteasome-independent. We demonstrate that D(d) targeted to the cytosol does not generate the Qa-1b peptide epitope even in the presence of lactacystin. Cells expressing herpes virus ICP-47 block the generation of this epitope, demonstrating that TAP functions in the transport of the peptide from cytosol to ER. This reveals a pathway for antigen presentation of leader peptides that involves translocation of a protein to the ER where its leader is cleaved followed by its release into the cytosol and transport back into the ER. Further, it ensures that Qa-1b expression mirrors the normal expression of class la molecules.
Original language | English (US) |
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Pages (from-to) | 413-421 |
Number of pages | 9 |
Journal | Immunity |
Volume | 9 |
Issue number | 3 |
DOIs | |
State | Published - Sep 1998 |
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology
- Infectious Diseases