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J. Exp. Med.,
Volume 187, Number 5, March 2, 1998 685-691
By



From the * Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77;
the Heat shock proteins (hsp's) isolated from murine cancer cells can elicit protective immunity
and specific cytotoxic T lymphocytes (CTLs) by channeling tumor-derived peptides bound to
hsp's to the major histocompatibility class I antigen presentation pathway. Here we have investigated if hsp70 can be used in a novel peptide vaccine for the induction of protective antiviral
immunity and memory CTLs. A CTL epitope from the well-defined lymphocytic choriomeningitis virus (LCMV) system was mixed with recombinant hsp70 in vitro under conditions that
optimize peptide binding to hsp70. Mice were immunized with the hsp70-peptide mixture
and challenged with LCMV. Virus titers were reduced 10-100-fold in these mice compared to
control mice. Immunization with the hsp70-peptide mixture resulted in the development of
CTL memory cells that could be reactivated during LCMV infection, and that in a 51Cr-release
assay could lyse cells pulsed with the same peptide, but not cells pulsed with another LCMV
peptide. These results show that hsp70 can be used with CTL epitopes to induce efficient protective antiviral immunity and the generation of peptide-specific CTLs. The results also demonstrate the usefulness of hsp70 as an alternative to adjuvants and DNA vectors for the delivery
of CTL epitopes to antigen-presenting cells.
Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts
01655; § Biogen, Inc., Cambridge, Massachusetts 02142;
NeoGenesis, Inc., Cambridge,
Massachusetts 02142; and the ¶ Department of Experimental Oncology, Radiumhemmet, Karolinska
Hospital, Stockholm, Sweden S-171 77
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