Transfer of GRP94(Gp96)-associated peptides onto endosomal MHC class I molecules.


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


  • eng

Conference Location

  • England