1887

Abstract

This study describes the purification and immunochemical characterization of a major 23 kDa cytosolic protein antigen of the vaccine candidate (TMC 5135). The 23 kDa protein alone was salted out from the cytosol at an ammonium sulfate saturation of 80-95%. It represented about 1.5% of the total cytosolic protein, appeared glycosylated by staining with periodic acid/Schiff's reagent, and showed a pl of approximately 5.3. Its native molecular mass was determined as approximately 48 kDa, suggesting a homodimeric configuration. Immunoblotting with the WHO-IMMLEP/IMMTUB mAbs mc5041 and IT61 and activity staining after native PAGE established its identity as a mycobacterial superoxide dismutase (SOD) of the Fe/Mn type. The sequence of the 18 N-terminal amino acids, which also contained the binding site for mc5041, showed a close resemblance, not only with the reported deduced sequences of and Fe/MnSODs, but also with human MnSOD. In order to study its immunopathological relevance, the protein was subjected to and assays for T cell activation. It induced, in a dose-related manner, skin delayed hypersensitivity in guinea-pigs and lymphocyte proliferation in BALB/c mice primed with Most significantly, it also induced lymphocyte proliferative responses, in a manner analogous to in human subjects comprising tuberculoid leprosy patients and healthy contacts.

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/content/journal/micro/10.1099/13500872-142-6-1375
1996-06-01
2019-11-13
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-142-6-1375
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