Heat shock protein-Peptide and HSP-based immunotherapies for the treatment of cancer

Maxim Shevtsov, Gabriele Multhoff

Research output: Contribution to journalShort surveypeer-review

137 Scopus citations


Intracellular residing heat shock proteins (HSPs) with a molecular weight of approximately 70 and 90 kDa function as molecular chaperones that assist folding/unfolding and transport of proteins across membranes and prevent protein aggregation after environmental stress. In contrast to normal cells, tumor cells have higher cytosolic heat shock protein 70 and Hsp90 levels, which contribute to tumor cell propagation, metastasis, and protection against apoptosis. In addition to their intracellular chaperoning functions, extracellular localized and membrane-bound HSPs have been found to play key roles in eliciting antitumor immune responses by acting as carriers for tumor-derived immunogenic peptides, as adjuvants for antigen presentation, or as targets for the innate immune system. The interaction of HSP-peptide complexes or peptide-free HSPs with receptors on antigen-presenting cells promotes the maturation of dendritic cells, results in an upregulation of major histocompatibility complex class I and class II molecules, induces secretion of pro- and anti-inflammatory cytokines, chemokines, and immune modulatory nitric oxides, and thus integrates adaptive and innate immune phenomena. Herein, we aim to recapitulate the history and current status of HSP-based immunotherapies and vaccination strategies in the treatment of cancer.

Original languageEnglish
Article number171
JournalFrontiers in Immunology
Issue numberAPR
StatePublished - 29 Apr 2016
Externally publishedYes


  • Adaptive immunity
  • Cancer vaccine
  • HSP70 heat shock proteins
  • HSP90 heat shock proteins
  • Innate immunity


Dive into the research topics of 'Heat shock protein-Peptide and HSP-based immunotherapies for the treatment of cancer'. Together they form a unique fingerprint.

Cite this