Heat shock proteins HSP70 and GP96: structural insights.
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.
Facciponte
John G
JG
Department of Immunology, Roswell Park Cancer Institute, Buffalo, NY 14263, USA. john.facciponte@roswellpark.org
Wang
Xiang-Yang
XY
MacDonald
Ian J
IJ
Park
Jun-eui
JE
Arnouk
Hilal
H
Grimm
Melissa J
MJ
Li
Ying
Y
Kim
Hyung
H
Manjili
Masoud H
MH
Easton
Douglas P
DP
Subjeck
John R
JR
D000818:Animals; D019496:Cancer Vaccines / Q000276:immunology; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000276:immunology*; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000276:immunology*; D009369:Neoplasms / Q000276:immunology*; D013329:Structure-Activity Relationship
D019496:Cancer Vaccines; D018840:HSP70 Heat-Shock Proteins; D008562:Membrane Glycoproteins; C053387:endoplasmin