Transfer of GRP94(Gp96)-associated peptides onto endosomal MHC class I molecules.
Published
Journal Article
GRP94 (gp96)-associated peptides can elicit cellular immune responses, an activity thought to reflect the presence of a cell surface receptor (CD91) on antigen-presenting cells that mediates GRP94 internalization and trafficking to an amenable site for peptide transfer to major histocompatibility complex class I molecules. We report that GRP94 internalized by receptor-mediated endocytosis is trafficked to a Rab5a, CD1 and transferrin-negative, Fc receptor and major histocompatibility complex class I-positive endocytic compartment. Receptor-internalized GRP94 did not access the endoplasmic reticulum of antigen-presenting cells. To identify the site of re-presentation of GRP94-associated peptides, kinetic analyses were performed utilizing GRP94-OVA (SIINFEKL) peptide complexes, with peptide re-presentation assayed with the Kb-SIINFEKL-specific MAb, 25-D1.16. Analyses of the kinetics of re-presentation of GRP94-associated peptides, under conditions in which de novo synthesis of major histocompatibility complex class I molecules was inhibited, identified a post-endoplasmic reticulum compartment, accessed by mature major histocompatibility complex class I, as the predominant site of GRP94-associated peptide exchange onto major histocompatibility complex class I.
Full Text
Duke Authors
Cited Authors
- Berwin, B; Rosser, MFN; Brinker, KG; Nicchitta, CV
Published Date
- May 2002
Published In
Volume / Issue
- 3 / 5
Start / End Page
- 358 - 366
PubMed ID
- 11967129
Pubmed Central ID
- 11967129
International Standard Serial Number (ISSN)
- 1398-9219
Digital Object Identifier (DOI)
- 10.1034/j.1600-0854.2002.30505.x
Language
- eng
Conference Location
- England