Immune Properties of HSP70

  • Yves DelnesteEmail author
  • Vincent Larochette
  • Pascale Jeannin
Part of the Heat Shock Proteins book series (HESP, volume 14)


In addition to their conventional chaperon activity, numerous studies have reported that heat shock protein 70 (HSP0) exhibit immune properties and especially the capacity (i) to induce the presentation and cross-presentation of associated or client proteins and, (ii) to control myeloid cell activation. Several studies were focused on the identification of HSP70-binding elements that contribute to their immune properties. A general consensus was reached on the nature of the endocytic receptors involved in the internalization of extracellular HSP70 with belong, for most of them, to the innate immunity receptor family. However, the nature of signaling receptors recruited by HSP70 remains unclear, because the stimulatory versus regulatory properties of HSP70 remains a subject of debate. Nevertheless, these unique immune properties allowed developing innovative prophylactic and therapeutic vaccines, especially in the treatment of cancers and chronic viral infections. Although HSP70 constitute potent vaccine vehicles in different preclinical models, clinical studies remain disappointing. The fact that the immune properties of HSP70 have not been totally clarified may explain their relative efficacy in human. In this review are presented the main immune properties of HSP70 related to the HSP70-binding elements identified to date, and discuss our current knowledge on their intrinsic immune properties.


Adaptive immunity Hsp70 Immune regulation Innate immune receptors Innate immunity Myeloid cell Vaccine 



alpha2 macroglobulin


acetylated low-density lipoprotein


adenosine dipohosphate


advanced glycation end product


apoptosis inducing factor


apoptotic peptidase activating factor 1


antigen-presenting cell


apolipoprotein E receptor


adenosine triphosphate


Bcl-2-associated X protein


B cell receptor


binding immunoglobulin protein


C-C motif ligand


C-C chemokine receptor


cluster of differentiation


C-type lectin domain family 8 member A


common lymphatic endothelial and vascular endothelial receptor-1


cytotoxic T cell


danger-associated molecular pattern


dendritic cell-specific ICAM-grabbing non-integrin


Epstein-Barr virus


and link domain-containing scavenger receptor-1


endoplasmic reticulum


Extracellular signal-regulated kinases


fatty acid translocase


fasciclin EGF-like laminin-type


hepatitis B virus


hepatitis C virus


human epidermal growth factor receptor 2/proto-oncogene Neu


human leukocyte antigen


high–mobility group box 1


human papilloma virus


heat shock protein






IL-1 receptor-associated kinase


inositol requiring enzyme 1α


Janus kinase


LPS-binding protein


low-density lipoprotein


low density lipoprotein receptor-related protein 1


melanoma-associated antigen 1


melanoma antigen recognized by T-cells 1


myeloid differentiation factor 2


myeloid-derived suppressive cells


major histocompatibility complex


Myeloid differentiation primary response 88


nucleotide-binding domain


nuclear factor-kappa B


natural killer


oxidized low-density lipoprotein


pathogen-associated molecular pattern


PDZ domain-containing protein 1


pattern recognition molecule


pattern recognition receptor


prostate-specific antigen


pentraxin 3


receptor-associated protein


substrate-binding domain


sialic-acid-binding immunoglobulin-like lectins


surfactant protein D


scavenger receptor expressed by endothelial cells


signal transducers and activators of transcription


TAK1-binding protein 1


TGFβ-activated kinase


tumor-associated macrophages


T cell receptor


helper T cell


toll-like receptor


tumor necrosis factor


TNF superfamily


TNF receptor-associated factor


tyrosinase-related protein 2


thrombospondin 1



Studies in our laboratory are supported by institutional grants from Inserm and the University of Angers and by grants from the Ligue contre le Cancer and the Cancéropole Grand Ouest. Vincent Larochette is supported by a grant fellowship from the French Ministry of Research and Higher Education. This manuscript was prepared in the context of the LabEX IGO program supported by the National Research Agency via the investment of the future program (ANR-11-LABEX-0016-01).


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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  • Yves Delneste
    • 2
    • 3
    • 1
    Email author
  • Vincent Larochette
    • 2
    • 3
  • Pascale Jeannin
    • 2
    • 3
    • 1
  1. 1.Laboratory of Immunology and AllergologyUniversity Hospital of AngersAngersFrance
  2. 2.CRCINA, INSERMUniversité de Nantes, Université d’AngersAngersFrance
  3. 3.LabEx ImmunoGraftOncoAngersFrance

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