Engineering secretable forms of chaperones for immune modulation and vaccine development

被引:12
作者
Beachy, S. H.
Kisalus, A. J.
Repasky, E. A.
Subjeck, J. R.
Wang, X. Y.
Kazim, A. L.
机构
[1] Roswell Pk Canc Inst, Dept Mol & Cellular Biophys & Biochem, Buffalo, NY 14263 USA
[2] Roswell Pk Canc Inst, Dept Immunol, Buffalo, NY 14263 USA
[3] Roswell Pk Canc Inst, Dept Cell Stress Biol, Buffalo, NY 14263 USA
关键词
heat shock protein; molecular chaperone; vaccine; anti-tumor; secreted; membrane bound; stress protein; protein engineering;
D O I
10.1016/j.ymeth.2007.06.001
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Heat shock proteins are present in almost all intracellular compartments and serve by folding newly synthesized proteins, disassembling unstable proteins, and assisting in the transportation of proteins within the cell. Under certain circumstances they are also present on the cell surface, and can be shed or secreted into the extracellular environment. Although they possess many functional roles, their ability to stimulate innate and antigen-specific immunity have made them attractive candidates for vaccine development. Here, we review some of the approaches that have been used to genetically engineer molecular chaperones for their secretion from tumor cells or targeting them to the plasma membrane of such cells in order to promote anti-tumor responses. Treatment of tumor cells engineered to secrete or display chaperones may be of benefit, particularly in the area of cell-based vaccine development. (C) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:184 / 193
页数:10
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