Single-Chain Fv-Based Affinity Purification of the Cellular Stress Protein gp96 for Vaccine Development.

Cellular stress proteins like the classical heat-shock proteins (HSPs) hsp70 (1-3), hsp90 (3) and hsp110 (4); the glucose-regulated proteins gp96/GRP94 (3,5) and grp170 (4); as well as the endoplasmic chaperone calreticulin (6,7) have been shown to induce cytotoxic T-cell responses and protective immunity when isolated from tumor or infected cells and used to vaccinate animals (8-10; reviewed in refs. 11-17). The specificity of the immune responses is owing to antigenic peptides associated with the HSPs (18-26). The HSP-peptide complexes are taken up by professional antigen-presenting cells (APCs) for effective presentation of the peptides to T cells (19,27-33). The extensively studied endoplasmic reticulum-resident chaperone gp96 is most efficient and promising in this regard (34-39); encouraging clinical studies with human cancer patients (40). [ABSTRACT FROM AUTHOR]