Testing the role of gp96 as peptide chaperone in antigen processing

doi:10.1074/jbc.M501233200

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Papers In Press, published online ahead of print February 23, 2005
J. Biol. Chem, 10.1074/jbc.M501233200
Submitted on February 2, 2005
Revised on February 18, 2005
Accepted on February 23, 2005

Testing the role of gp96 as peptide chaperone in antigen processing

Rodion Demine and Peter Walden

Department of Dermatology, Charité - University Medicine Berlin, Berlin D-10117

Corresponding Author: peter.walden{at}charite.de

Gp96 is a 96 kDa glycoprotein of the endoplasmic reticulum (ER) which is believed to be involved in antigen processing as intermediate carrier of peptides for presentation by MHC class I molecules. This function implies that gp96 carries a large array of different peptides that represent the antigenicity of the cell and can serve all MHC class I molecules. So far, the evidence regarding these peptides is largely indirect and based on experiments where mice immunized with gp96 from tumor or virus-infected cells developed T-cellular immune responses with the corresponding specificities. We analyzed by mass spectrometry peptides isolated from gp96 and found a number of different peptides derived from proteins of different cellular compartments but mostly cytoplasm and nucleus. The sequences of these peptides provide information on the specificity of antigen processing and reveal structural requirements for binding to gp96 which only partially correspond to those of peptides presented by MHC class I molecules. The yield of peptides extracted from gp96 was far substoichiometric with an estimated occupancy of this chaperone of below 1%. These results strongly argue against a regular role of gp96 as a peptide chaperone in antigen processing.

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