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J. Biol. Chem., Vol. 276, Issue 20, 17163-17171, May 18, 2001
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From the Center for Immunotherapy of Cancer and Infectious
Diseases, University of Connecticut School of Medicine, Farmington,
Connecticut 06030
The studies reported here bear on the events in
the cytosol that lead to trafficking of peptides during antigen
processing and presentation by major histocompatibility complex (MHC) I
molecules. We have introduced free antigenic peptides or antigenic
peptides bound to serum albumin or to cytosolic heat shock proteins
hsp90 (and its endoplasmic reticular homologue gp96) or hsp70 into the cytosol of living cells and have monitored the presentation of the
peptides by appropriate MHC I molecules. The experiments show that (i)
free peptides or serum albumin-bound peptides, introduced into the
cytosol, become ligands of MHC I molecules at a far lower efficiency
than peptides chaperoned by any of the heat shock proteins tested and
(ii) treatment of cells with deoxyspergualin, a drug that binds hsp70
and hsp90 with apparent specificity, abrogates the ability of cells to
present antigenic peptides through MHC I molecules, and introduction of
additional hsp70 into the cytosol overcomes this abrogation. These
results suggest for the first time a functional role for cytosolic
chaperones in antigen processing.
Heat Shock Protein-chaperoned Peptides but Not Free Peptides
Introduced into the Cytosol Are Presented Efficiently by Major
Histocompatibility Complex I Molecules*
,§, and
*
This work was supported by National Institutes of Health
Grants CA64394 and CA44786, Defense Advanced Research Project
Agency Grant BAA96024, and a research agreement with Antigenics,
Inc, in which company one of us (P. K. S.) has a significant
financial interest.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Both authors contributed equally to this work.
§
Present address: Memorial Sloan-Kettering Cancer Center, New York,
NY 10021.
¶
To whom correspondence should be addressed: School of
Medicine, MC1601, University of Connecticut, Farmington, CT 06030-1920. Tel.: 860-679-4444; Fax: 860-679-4365; E-mail:
srivastava@nso2.uchc.edu.
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