PMID: 9425150Feb 14, 1998Paper

Surrogate antigen processing mediated by TAP-dependent antigenic peptide secretion

The Journal of Cell Biology
R GabathulerW A Jefferies

Abstract

MHC class I proteins assemble with peptides in the ER. The peptides are predominantly generated from cytoplasmic proteins, probably by the action of the proteasome, a multicatalytic proteinase complex. Peptides are translocated into the ER by the transporters associated with antigen processing (TAP), and bind to the MHC class I molecules before transport to the cell surface. Here, we use a new functional assay to demonstrate that peptides derived from vesicular stomatitis virus nucleoprotein (VSV-N) antigen are actively secreted from cells. This secretion pathway is dependent on the expression of TAP transporters, but is independent of the MHC genotype of the donor cells. Furthermore, the expression and transport of MHC class I molecules is not required. This novel pathway is sensitive to the protein secretion inhibitors brefeldin A (BFA) and a temperature block at 21 degrees C, and is also inhibited by the metabolic poison, azide, and the protein synthesis inhibitor, emetine. These data support the existence of a novel form of peptide secretion that uses the TAP transporters, as opposed to the ER translocon, to gain access to the secretion pathway. Finally, we suggest that this release of peptides in the vicinity of uninfected...Continue Reading

References

Nov 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·S BahramT Spies
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Citations

Feb 2, 1999·Journal of Peptide Science : an Official Publication of the European Peptide Society·R BarboucheE Fenouillet
Feb 27, 1999·Current Opinion in Immunology·P M van Endert
Dec 20, 2005·FEBS Letters·Rupert Abele, Robert Tampé
Feb 26, 2003·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·Karl Erik Hellstrom, Ingegerd Hellstrom

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