The pathway for processing leader-derived peptides that regulate the maturation and expression of Qa-1b

Ailin Bai, James Broen, James Forman

Research output: Contribution to journalArticle

30 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)413-421
Number of pages9
JournalImmunity
Volume9
Issue number3
DOIs
StatePublished - Jan 1 1998

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Protein Sorting Signals
Cytosol
Epitopes
Peptides
Antigen Presentation
Protein Transport
Proteasome Endopeptidase Complex
Viruses

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

Cite this

The pathway for processing leader-derived peptides that regulate the maturation and expression of Qa-1b . / Bai, Ailin; Broen, James; Forman, James.

In: Immunity, Vol. 9, No. 3, 01.01.1998, p. 413-421.

Research output: Contribution to journalArticle

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