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International Immunology Advance Access originally published online on June 13, 2006
International Immunology 2006 18(7):1147-1157; 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

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

Chhanda Biswas1, Uma Sriram2, Bogoljub Ciric1, Olga Ostrovsky1, Stefania Gallucci2 and Yair Argon1

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

Correspondence to: Y. Argon; E-mail: yargon{at}mail.med.upenn.edu

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

Transmitting editor: A. Singer


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