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International Immunology Advance Access published online on June 13, 2006
International Immunology, doi:10.1093/intimm/dxl049
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© The Japanese Society for Immunology. 2006. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received February 7, 2006
Accepted April 27, 2006

Article

The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells

Chhanda Biswas 1, Uma Sriram 2, Bogoljub Ciric 1, Olga Ostrovsky 1, Stefania Gallucci 2, and Yair Argon 1 *

1 Department of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104, USA
2 Department of Pediatrics, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104, USA

* To whom correspondence should be addressed.
Yair Argon, E-mail: yargon{at}mail.med.upenn.edu


  Abstract

The chaperone glucose-regulated protein 94 (GRP94) has long been used to augment peptide presentation to T cells. This chaperone binds antigenic peptides, binds to receptors on professional antigen-presenting cells (APCs), activates these cells and after internalization, transfers the peptides to MHC class I for activation of T cells. Here we show that all these activities reside within amino acids 1-355 of GRP94. This small fragment is sufficient to bind peptides, to bind and be taken up by the receptors CD91 and scavenger receptor type A on either dendritic cells or macrophages. The minimal construct can augment peptide presentation in culture and induce antigen-specific CTL in naive mice only because it loads APCs with the relevant peptide. Thus, the sequence 1-355 is the immunologically sufficient module of GRP94 and we propose that this ‘mini-chaperone’ can be used in immunotherapy of tumors and vaccine development.

Keywords: antigen presentation; cross presentation; dendritic cells; macrophages; molecular chaperones; peptide binding.
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