The Study of Complex Formation of Human Recombinant HSP70 with Tumor-Associated Peptides

摘要

Molecular chaperones of the HSP70 family (70 kDa heat shock proteins) are involved in presentation of exogenous antigenic peptides by antigen-presenting cells (APC). HSP70 complexes with tumor-associated peptides are powerful immunotherapeutic agents, inducing an adaptive cytotoxic T-cell mediated immune response. Several clinical trials have shown that HSP-based autological anticancer vaccines possess high efficiency and safety. However, sometimes it is impossible to isolate sufficient amount of such vaccines and so human recombinant HSP are used for in vitro loading with tumor-associated peptides. In this study we have investigated binding of two human recombinant proteins HSP70_(HYB) and HSC70 with antigenic peptides of different origin and optimized conditions for complex formation. The proposed method for complex formation increases the repertoire of HSP70 bound peptides compared with in vivo formed complexes.