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,
*
Department of Pathobiology, University of Washington, Seattle, WA 98195; and
Infectious Disease Research Institute and
CORIXA Corporation, Seattle, WA 98104
Polypeptide Ags present in the culture filtrate of
Mycobacterium tuberculosis were purified and evaluated
for their ability to stimulate PBMC from purified protein derivative
(PPD)-positive healthy donors. One such Ag, which elicited strong
proliferation and IFN-
production, was further characterized. The
N-terminal amino acid sequence of this polypeptide was determined and
used to design oligonucleotides for screening a recombinant M.
tuberculosis genomic DNA library. The gene (Mtb
8.4) corresponding to the identified polypeptide was cloned,
sequenced, and expressed in Escherichia coli. The
predicted m.w. of the recombinant protein without its signal peptide
was 8.4 kDa. By Southern analysis, the DNA encoding this mycobacterial
protein was found in the M. tuberculosis substrains
H37Rv, H37Ra, Erdman, and "C" strain, as well as in certain other
mycobacterial species, including Mycobacterium avium and
Mycobacterium bovis BCG (bacillus Calmette-Guérin,
Pasteur). The Mtb 8.4 gene appears to be absent from the
environmental mycobacterial species examined thus far, including
Mycobacterium smegmatis, Mycobacterium
gordonae, Mycobacterium chelonae,
Mycobacterium fortuitum, and Mycobacterium
scrofulaceum. Recombinant Mtb 8.4 Ag induced significant
proliferation as well as production of IFN-, IL-10, and TNF-
, but
not IL-5, from human PBMC isolated from PPD-positive healthy donors.
Mtb 8.4 did not stimulate PBMC from PPD-negative donors. Furthermore,
immunogenicity studies in mice indicate that Mtb 8.4 elicits a Th1
cytokine profile, which is considered important for protective immunity
to tuberculosis. Collectively, these results demonstrate that Mtb 8.4
is an immunodominant T cell Ag of M.
tuberculosis.
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