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* Peter Gorer Department of Immunobiology, and
Department of Oral Medicine and Pathology, Guy’s, King’s, & St. Thomas’ Hospital Medical and Dental Schools, London, United Kingdom;
Lionex Diagnostics and Therapeutics, Braunschweig, Germany
The peptide binding C-terminal portion of heat shock protein
(HSP)70 (aa 359–610) stimulates human monocytes to produce IL-12,
TNF-
, NO, and C-C chemokines. The N-terminal, ATPase portion
(HSP701–358) failed to stimulate any of these cytokines or
chemokines. Both native and the truncated HSP70359–610
stimulation of chemokine production is mediated by the CD40
costimulatory molecule. Maturation of dendritic cells was induced by
stimulation with native HSP70, was not seen with the N-terminal
HSP701–358, but was enhanced with
HSP70359–610, as demonstrated by up-regulation of CD83,
CCR7, CD86, CD80, and HLA class II. In vivo studies in macaques showed
that immunization with HSP70359–610 enhances the
production of IL-12 and RANTES. Immunization with peptide-bound
HSP70359–610 in mice induced higher serum IgG2a and IgG3
Abs than the native HSP70-bound peptide. This study suggests that the
C-terminal, peptide-binding portion of HSP70 is responsible for
stimulating Th1-polarizing cytokines, C-C chemokines, and an adjuvant
function.
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