02783nas a2200469   4500000000100000008004100001260001600042653002400058653001200082653002400094653001500118653002200133653002300155653001900178653001700197653002100214653002400235653001100259653001200270653002800282653002100310653002500331653002500356653002400381653003600405653001800441100001200459700001400471700001600485700001500501700001600516700001300532700001300545700001200558700001500570700001600585245009000601300001100691490000800702520158900710022001402299       1992                            d  c1992 Jan 0110aAmino Acid Sequence10aAnimals10aAntigens, Bacterial10aArmadillos10aBlotting, Western10aCloning, Molecular10aDNA, Bacterial10aGene Library10aGenes, Bacterial10aHeat-Shock Proteins10aHumans10aleprosy10aMolecular Sequence Data10aMolecular Weight10aMycobacterium leprae10aRecombinant Proteins10aRestriction Mapping10aSequence Homology, Nucleic Acid10aT-Lymphocytes1 aMehra V1 aBloom B R1 aBajardi A C1 aGrisso C L1 aSieling P A1 aAlland D1 aConvit J1 aFan X D1 aHunter S W1 aBrennan P J00aA major T cell antigen of Mycobacterium leprae is a 10-kD heat-shock cognate protein.  a275-840 v1753 a<p>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.</p>  a0022-1007