期刊
INTERNATIONAL IMMUNOLOGY
卷 18, 期 7, 页码 1147-1157出版社
OXFORD UNIV PRESS
DOI: 10.1093/intimm/dxl049
关键词
antigen presentation; cross presentation; dendritic cells; macrophages; molecular chaperones; peptide binding
类别
资金
- NIAID NIH HHS [AI-049892] Funding Source: Medline
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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