TY - JOUR KW - Amino Acid Sequence KW - Animals KW - Antigens, Bacterial KW - Armadillos KW - Blotting, Western KW - Cloning, Molecular KW - DNA, Bacterial KW - Gene Library KW - Genes, Bacterial KW - Heat-Shock Proteins KW - Humans KW - leprosy KW - Molecular Sequence Data KW - Molecular Weight KW - Mycobacterium leprae KW - Recombinant Proteins KW - Restriction Mapping KW - Sequence Homology, Nucleic Acid KW - T-Lymphocytes AU - Mehra V AU - Bloom B R AU - Bajardi A C AU - Grisso C L AU - Sieling P A AU - Alland D AU - Convit J AU - Fan X D AU - Hunter S W AU - Brennan P J AB -

Several mycobacterial antigens, identified by monoclonal antibodies and patient sera, have been found to be homologous to stress or heat-shock proteins (hsp) defined in Escherichia coli and yeast. A major antigen recognized by most Mycobacterium leprae-reactive human T cell lines and cell wall-reactive T cell clones is a 10-kD protein that has now been cloned and sequenced. The predicted amino acid sequence of this protein is 44% homologous to the hsp 10 (GroES) of E. coli. The purified native and recombinant 10-kD protein was found to be a stronger stimulator of peripheral blood T cell proliferation than other native and recombinant M. leprae proteins tested. The degree of reactivity paralleled the response to intact M. leprae throughout the spectrum of leprosy. Limiting-dilution analysis of peripheral blood lymphocytes from a patient contact and a tuberculoid patient indicated that approximately one third of M. leprae-reactive T cell precursors responded to the 10-kD antigen. T cell lines derived from lepromin skin tests were strongly responsive to the 10-kD protein. T cell clones reactive to both the purified native and recombinant 10-kD antigens recognized M. leprae-specific epitopes as well as epitopes crossreactive with the cognate antigen of M. tuberculosis. Further, the purified hsp 10 elicited strong delayed-type hypersensitivity reactions in guinea pigs sensitized to M. leprae. The strong T cell responses against the M. leprae 10-kD protein suggest a role for this heat-shock cognate protein in the protective/resistant responses to infection.

BT - The Journal of experimental medicine C1 - http://www.ncbi.nlm.nih.gov/pubmed/1730920?dopt=Abstract DA - 1992 Jan 01 DO - 10.1084/jem.175.1.275 IS - 1 J2 - J. Exp. Med. LA - eng N2 -

Several mycobacterial antigens, identified by monoclonal antibodies and patient sera, have been found to be homologous to stress or heat-shock proteins (hsp) defined in Escherichia coli and yeast. A major antigen recognized by most Mycobacterium leprae-reactive human T cell lines and cell wall-reactive T cell clones is a 10-kD protein that has now been cloned and sequenced. The predicted amino acid sequence of this protein is 44% homologous to the hsp 10 (GroES) of E. coli. The purified native and recombinant 10-kD protein was found to be a stronger stimulator of peripheral blood T cell proliferation than other native and recombinant M. leprae proteins tested. The degree of reactivity paralleled the response to intact M. leprae throughout the spectrum of leprosy. Limiting-dilution analysis of peripheral blood lymphocytes from a patient contact and a tuberculoid patient indicated that approximately one third of M. leprae-reactive T cell precursors responded to the 10-kD antigen. T cell lines derived from lepromin skin tests were strongly responsive to the 10-kD protein. T cell clones reactive to both the purified native and recombinant 10-kD antigens recognized M. leprae-specific epitopes as well as epitopes crossreactive with the cognate antigen of M. tuberculosis. Further, the purified hsp 10 elicited strong delayed-type hypersensitivity reactions in guinea pigs sensitized to M. leprae. The strong T cell responses against the M. leprae 10-kD protein suggest a role for this heat-shock cognate protein in the protective/resistant responses to infection.

PY - 1992 SP - 275 EP - 84 T2 - The Journal of experimental medicine TI - A major T cell antigen of Mycobacterium leprae is a 10-kD heat-shock cognate protein. VL - 175 SN - 0022-1007 ER -