Journal
INTERNATIONAL IMMUNOLOGY
Volume 18, Issue 7, Pages 1147-1157Publisher
OXFORD UNIV PRESS
DOI: 10.1093/intimm/dxl049
Keywords
antigen presentation; cross presentation; dendritic cells; macrophages; molecular chaperones; peptide binding
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Funding
- NIAID NIH HHS [AI-049892] Funding Source: Medline
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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.
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