TY - JOUR KW - Amino Acid Sequence KW - Animals KW - Antibodies, Bacterial KW - Antibodies, Monoclonal KW - Antigens, Bacterial KW - Bacterial Proteins KW - Chromatography, Affinity KW - Cytochrome b Group KW - Ferritins KW - Humans KW - leprosy KW - Molecular Sequence Data KW - Molecular Weight KW - Mycobacterium avium subsp. paratuberculosis KW - Mycobacterium leprae KW - Rabbits KW - Sequence Homology, Amino Acid AU - Deshpande R G AU - Khan M B AU - Bhat D A AU - Navalkar R G AB -

The purpose of this study was to isolate Mycobacterium leprae antigen(s) by immunoaffinity chromatography using immunoglobulins from leprosy patients and from rabbit anti-M. leprae hyperimmune serum coupled to CNBr-Sepharose 4B. A high molecular weight (M(r)) M. leprae protein (MLP) with a subunit M(r) of 22,000 was isolated. MLP was recognized by monoclonal antibody MMPII1G4 which is known to react with MMPII, a 22 kDa protein of M. leprae. The N-terminal sequence of the 22 kDa subunit (Met-gln-gly-asp-pro-asp-val-leu-arg-leu-leu-asn-glu-gln-leu-thr) was identical to MMPII and to antigen D (bacterioferritin) of M. paratuberculosis. It showed 44% homology with N-terminal end of E. coli bacterioferritin. In ELISA, MLP showed 100% and 60% positivity with leprosy and TB sera respectively as compared to normal healthy sera. The role of bacterioferritin in M. leprae and the importance of MLP as an immunogen has been discussed.

BT - FEMS immunology and medical microbiology C1 - http://www.ncbi.nlm.nih.gov/pubmed/7581267?dopt=Abstract DA - 1995 Jun DO - 10.1111/j.1574-695X.1995.tb00113.x IS - 3 J2 - FEMS Immunol. Med. Microbiol. LA - eng N2 -

The purpose of this study was to isolate Mycobacterium leprae antigen(s) by immunoaffinity chromatography using immunoglobulins from leprosy patients and from rabbit anti-M. leprae hyperimmune serum coupled to CNBr-Sepharose 4B. A high molecular weight (M(r)) M. leprae protein (MLP) with a subunit M(r) of 22,000 was isolated. MLP was recognized by monoclonal antibody MMPII1G4 which is known to react with MMPII, a 22 kDa protein of M. leprae. The N-terminal sequence of the 22 kDa subunit (Met-gln-gly-asp-pro-asp-val-leu-arg-leu-leu-asn-glu-gln-leu-thr) was identical to MMPII and to antigen D (bacterioferritin) of M. paratuberculosis. It showed 44% homology with N-terminal end of E. coli bacterioferritin. In ELISA, MLP showed 100% and 60% positivity with leprosy and TB sera respectively as compared to normal healthy sera. The role of bacterioferritin in M. leprae and the importance of MLP as an immunogen has been discussed.

PY - 1995 SP - 163 EP - 9 T2 - FEMS immunology and medical microbiology TI - Immunoaffinity chromatographic isolation of a high molecular weight seroreactive protein from Mycobacterium leprae cell sonicate. VL - 11 SN - 0928-8244 ER -