Heat shock protein 70-peptide complex (HSP70-PC)

The Heat shock protein 70-peptide complex (HSP70-PC) is a molecular assembly consisting of the chaperone protein HSP70 (primarily HSPA1A/B) non-covalently bound to a diverse repertoire of tumor-derived antigenic peptides (Blachere et al., 1997; NIH, 1.2.1). In the context of cancer immunotherapy, these complexes are typically purified from a patient's own tumor tissue to create an autologous vaccine, such as those tested in clinical trials for chronic myeloid leukemia (NCT00027144; NIH, 1.2.3). The biological function of the complex involves the delivery of tumor antigens to professional antigen-presenting cells (APCs), such as dendritic cells, through specific receptors like CD91, LOX-1, or CD14/TLR2/4 (ResearchGate, 1.1.1; MDPI, 1.3.4). Once internalized, the chaperoned peptides are processed and cross-presented on MHC class I and II molecules, leading to the activation of tumor-specific CD8+ and CD4+ T cells (Encyclopedia.pub, 1.2.1). Additionally, extracellular HSP70 acts as a "chaperokine," stimulating the innate immune system by inducing the release of pro-inflammatory cytokines like TNF-alpha and IL-6 (Cambridge, 1.1.4). Therapeutic strategies utilizing HSP70-peptide complexes have been investigated in various malignancies, including melanoma and glioblastoma, demonstrating a favorable safety profile and the ability to induce specific anti-tumor immunity (MDPI, 1.3.1).

Other names

HSP70-peptide complexAutologous tumor-derived HSP70-peptide complexHSPA1-peptide complexTumor-derived HSP70-peptide complexHSP70-PC-F

Induction of tumor-specific T-cell responses through receptor-mediated uptake by antigen-presenting cells and subsequent cross-presentation of chaperoned peptides on MHC molecules.