The Journal of Experimental Medicine
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© The Rockefeller University Press, 0022-1007/2000/1/403/ $5.00
The Journal of Experimental Medicine, Volume 191, Number 2, January 17, 2000 403-408

Brief Definitive Report

In Vivo Cytotoxic T Lymphocyte Elicitation by Mycobacterial Heat Shock Protein 70 Fusion Proteins Maps to a Discrete Domain and Is Cd4+ T Cell Independent

Qian Huanga, Joan F.L. Richmonda, Kimiko Suzuea, Herman N. Eisenb,c, and Richard A. Younga,b

a Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142
b Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
c Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142.617-258-0376617-258-5218

young{at}wi.mit.edu

To gain insights into the mechanisms by which soluble heat shock protein (hsp) fusions can elicit CD8+ cytotoxic T lymphocytes (CTLs) against the fusion partner, mycobacterial (Mycobacterium tuberculosis) hsp70 was dissected to ascertain whether a particular hsp domain is necessary, and knockout mice were used to determine whether the fusion protein's immunogenicity is dependent on CD4+ T lymphocytes. We found that the ability to elicit CD8+ CTLs depends on a discrete 200–amino acid protein domain, indicating that the fusion protein's immunogenicity for CD8+ T cells does not require coupled chaperone function or peptide binding. Further, we found that ovalbumin (OVA).hsp70 fusion protein elicited anti-OVA CD8+ CTLs about equally well in CD4 knockout and wild-type C57BL/6 mice, and also when the hsp70 was of murine (self) origin. The ability of hsp70 fusion proteins to elicit CD4-independent CTL responses suggests that hsp70 fusion proteins may be useful for immunological prophylaxis and therapy against disease in CD4+ T cell–deficient individuals.

Key Words: CD8+ • CD4+ • domain • knockout • vaccine

Q. Huang and J.F.L. Richmond contributed equally to this work.

© 2000 The Rockefeller University Press


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