The Journal of Experimental Medicine
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text
Right arrow Full Text (PDF, 129K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JEM
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Basu, S.
Right arrow Articles by Srivastava, P. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Basu, S.
Right arrow Articles by Srivastava, P. K.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?
© The Rockefeller University Press, 0022-1007/1999/3/797/ $5.00
The Journal of Experimental Medicine, Volume 189, Number 5, March 1, 1999 797-802


Articles

Calreticulin, a Peptide-binding Chaperone of the Endoplasmic Reticulum, Elicits Tumor- and Peptide-specific Immunity

Sreyashi Basu and Pramod K. Srivastava

From the Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut 06030

Calreticulin (CRT), a peptide-binding heat shock protein (HSP) of the endoplasmic reticulum (ER), has been shown previously to associate with peptides transported into the ER by transporter associated with antigen processing (Spee, P., and J. Neefjes. 1997. Eur. J. Immunol. 27: 2441–2449). Our studies show that CRT preparations purified from tumors elicit specific immunity to the tumor used as the source of CRT but not to an antigenically distinct tumor. The immunogenicity is attributed to the peptides associated with the CRT molecule and not to the CRT molecule per se. It is further shown that CRT molecules can be complexed in vitro to unglycosylated peptides and used to elicit peptide-specific CD8+ T cell response in spite of exogenous administration. These characteristics of CRT closely resemble those of HSPs gp96, hsp90, and hsp70, although CRT has no apparent structural homologies to them.

Key Words: heat shock protein • stress protein • antigen presentation • cytotoxic T lymphocyte response • cancer immunity


Address correspondence to Pramod K. Srivastava, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, MC1601, Farmington, CT 06030. Phone: 860-679-4444; Fax: 860-679-4365; E-mail: srivastava{at}nso2.uchc.edu

Note added in proof. During the course of these studies, we have learned that C. Nicchita, E. Gilboa, and colleagues have independently discovered that calreticulin can elicit, in a cell- and tumor-specific manner, CTL responses (Nair, S., P. Wearsch, D.A. Mitchell, J.J. Wassenberg, E. Gilboa, and C.V. Nicchita. Calreticulin displays in vivo peptide binding activity and can elicit cytotoxic T lymphocyte responses against bound peptides. J. Immunol. In press.).

Abbreviations used: CRT, calreticulin; ER, endoplasmic reticulum; HSP, heat shock protein; PDI, protein disulfide isomerase; TAP, transporter associated with antigen processing; VSV, vesicular stomatitis virus.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search
TABLE OF CONTENTS