Heat-shock proteins as activators of the innate immune system.
Peptides bound or linked to heat-shock proteins (HSPs) of microbial or mammalian origin have been shown to elicit potent antigen-specific immunity. Some members of the HSP family, such as hsp60, hsp70, hsp90 and gp96, are able also to stimulate cells of the innate immune system directly and thus, act as 'danger'-signaling molecules. This effect is independent of HSP-associated peptides and, in many respects, resembles the effect of lipopolysaccharide (LPS). Here, we discuss the similarities between the responses to HSPs and LPS and also, emphasize that care must be taken when working with preparations of HSPs in experimental settings and interpreting experimental data.
Wallin
Robert P A
RP
Microbiology and Tumor Biology Center, Karolinska Institutet, S-171 77, Stockholm, Sweden. robert.wallin@mtc.ki.se
Lundqvist
Andreas
A
Moré
Solveig H
SH
von Bonin
Arne
A
Kiessling
Rolf
R
Ljunggren
Hans-Gustaf
HG
D000818:Animals; D000938:Antigen-Presenting Cells / Q000276:immunology; D001426:Bacterial Proteins / Q000494:pharmacology; D018834:Chaperonin 60 / Q000502:physiology; D006360:Heat-Shock Proteins / Q000502:physiology*; D018869:Heat-Shock Response / Q000187:drug effects; D007113:Immunity, Innate; D008070:Lipopolysaccharides / Q000494:pharmacology; D018448:Models, Immunological; D015398:Signal Transduction
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D008070:Lipopolysaccharides