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Bernhard-Nocht-Institute for Tropical Medicine, Hamburg, Germany
Heat shock proteins (HSP) Hsp70 and gp96 prime class I-restricted
cytotoxic T cells against Ags present in the cells from which they were
isolated. The immunization capacity of HSPs is believed to rely on
their ability to bind antigenic peptides. In this study, we employed
the well-established OVA and ß-galactosidase (ß-gal) antigenic
model systems. We show that in vitro long-term established OVA and
ß-gal-specific CTL clones release TNF-
and IFN-
when incubated
with Ag-negative Hsp70 and gp96. In the absence of antigenic peptides,
HSP-mediated secretion of TNF- and IFN- requires cell contact of
the APC with the T cell but is not MHC-I restricted. Moreover, Hsp70
molecules purified from Ag-negative tissue, e.g., negative for
antigenic peptide, are able to activate T cells in vivo, leading to
significant higher frequencies in OVA-specific CD8+ T
cells. In unprimed animals, these T cells lyse OVA-transfected cell
lines and produce TNF- and IFN- after Ag stimulus. Taken together
our data show that, besides the well-established HSP/peptide-specific
CTL induction and activation, a second mechanism exists by which Hsp70
and gp96 molecules activate T cells in vivo and in
vitro.
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