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J. Biol. Chem., Vol. 276, Issue 36, 33313-33318, September 7, 2001
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From the gp96, an abundant peptide-binding chaperone of
the lumen of the endoplasmic reticulum and an acceptor of peptides
transported into the endoplasmic reticulum through transporter
associated with antigen processing, is shown to be an aminopeptidase.
gp96 can trim an amino-terminal extended 19-mer precursor of the
Kb-binding VSV8 epitope for recognition by the
cognate cytotoxic T lymphocyte clone. These observations support
a role for gp96 in the amino-terminal trimming of extended peptides in
the endoplasmic reticulum.
An Endoplasmic Reticulum Protein Implicated in Chaperoning
Peptides to Major Histocompatibility of Class I Is an
Aminopeptidase*
,,
Center for Immunotherapy of Cancer and
Infectious Diseases (MC1601), University of Connecticut School of
Medicine, Farmington, Connecticut 06030, § Antigenics Inc.,
Woburn, Massachusetts 01801, and ¶ Cornell University, New
York, New York 10021
*
This work (at the University of Connecticut) was supported
by National Institutes of Health Grants CA-64394 and CA-44786 and by a
research agreement with Antigenics (in which 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.
To whom correspondence should be addressed: Center for
Immunotherapy (MC1601), University of Connecticut School of Medicine, Farmington, CT 06030. Tel.: 860-679-4444; Fax: 860-679-4365, E-mail: srivastava@nso2.uchc.edu.
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