Heat shock protein 70-peptide complex (HSPPC-70) (HSPPC-70)

Tumor-associated antigens (TAAs) chaperoned by Heat Shock Protein 70 (HSP70), known as HSPPC-70, represent a class of personalized cancer immunotherapies. HSP70 is a molecular chaperone that naturally binds to a broad repertoire of intracellular peptides, including those derived from mutated or overexpressed proteins in cancer cells (Srivastava, P. K., 2002, Annu Rev Immunol). These complexes are typically purified from a patient's own tumor tissue to create an autologous vaccine, capturing the unique antigenic profile of that individual's malignancy (NCI Drug Dictionary, 2024). Upon administration, the HSP70 component acts as an adjuvant by binding to the CD91 receptor (LRP1) on professional antigen-presenting cells (APCs) (Binder, R. J., 2000, Nat Immunol). This interaction facilitates the internalization of the complex and the subsequent cross-presentation of the tumor-specific peptides on MHC Class I and II molecules. This process triggers a robust, multi-antigenic T-cell response directed specifically against the patient's tumor cells (Manjili, M. H., et al., 2002, Cancer Res). Clinical development has primarily focused on autologous preparations like Vitespen (Oncophage) for various malignancies, including renal cell carcinoma and glioma (Wood, C., et al., 2008, Lancet).

Other names

Tumor-derived HSP70-peptide complexVitespenOncophageHSP70-TAA complexTumor-associated antigens chaperoned by HSP70

Binding to CD91 (LRP1) receptors on antigen-presenting cells to facilitate the internalization and cross-presentation of tumor-specific peptides to T-cells (Srivastava, P. K., 2002, Annu Rev Immunol).