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Heat shock proteins HSP70 and GP96: structural insights

  • Symposium in Writing
  • Published:
Cancer Immunology, Immunotherapy Aims and scope Submit manuscript

Abstract

Several heat shock proteins (HSPs) act as potent adjuvants for eliciting anti-tumor immunity. HSP-based tumor vaccine strategies have been highly successful in animal models and are undergoing testing in clinical trials. It is generally accepted that HSPs, functioning as chaperones for tumor antigens, elicit tumor-specific adaptive immune responses. HSPs also appear to induce innate immune responses in an antigen-independent fashion. Innate responses generated by HSPs may contribute to anti-tumor immunity. Immunologically active chaperones with anti-tumor activity are referred to as “immunochaperones”. Here, we review the studies that address the role of structural domains or regions of the immunochaperones HSP70 and GP96 that may be involved in the induction of adaptive or innate immune responses.

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Abbreviations

APCs:

Antigen presenting cells

CTD:

C-terminal domain

CTL:

Cytotoxic T lymphocyte

DCs:

Dendritic cells

HSPs:

Heat shock proteins

IFN:

Interferon

LPS:

Lipopolysaccharide

LOX-1:

Lectin-like oxidized low-density lipoprotein receptor

MHC:

Major histocompatibility complex

NK:

Natural killer

NO:

Nitric oxide

NTD:

N-terminal domain

PBD:

Peptide-binding domain

PRR:

Pattern recognition receptor

RANTES:

Regulated on activation, normal T expressed and secreted

SR-A:

Scavenger receptor-A

TLR:

Toll-like receptor

TNF:

Tumor necrosis factor

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Acknowledgements

This work was supported by NIH grants RO-1 CA099326-13, PO-1 CA94045-01A2SUB (JRS) and by shared resources of the Roswell Park Cancer Center Support Grant P30 CA16056, as well as a Department of Defense Pre-Doctoral Grant (JGF). Views and opinions of, and endorsements by the author(s) do not reflect those of the US Army or the Department of Defense.

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Authors and Affiliations

  1. Department of Immunology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA

    John G. Facciponte & Ying Li

  2. Department of Cellular Stress Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA

    Xiang-Yang Wang, Ian J. MacDonald, Melissa J. Grimm & John R. Subjeck

  3. Department of Pathology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA

    Hilal Arnouk

  4. Department of Surgery, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA

    Hyung Kim

  5. Department of Urology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA

    Xiang-Yang Wang & Hyung Kim

  6. Department of Medicine and Swim Across America Laboratory, Memorial Sloan-Kettering Cancer Center, 1275 York Ave., New York, NY, 10021, USA

    Jun-eui Park

  7. Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, VA, 23284, USA

    Masoud H. Manjili

  8. Department of Biology, State University of New York, College at Buffalo, Buffalo, NY, 14222, USA

    Douglas P. Easton

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  1. John G. Facciponte
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  2. Xiang-Yang Wang
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  11. John R. Subjeck
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Correspondence to John G. Facciponte.

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This article forms part of the Symposium in Writing “Thermal stress-related modulation of tumor cell physiology and immune responses”, edited by Elfriede Noessner.

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Facciponte, J.G., Wang, XY., MacDonald, I.J. et al. Heat shock proteins HSP70 and GP96: structural insights. Cancer Immunol Immunother 55, 339–346 (2006). https://doi.org/10.1007/s00262-005-0020-y

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