Deshpande R G, Khan M B, Bhat D A, Navalkar R G
Department of Microbiology and Immunology, Morehouse School of Medicine, Atlanta, GA 30310, USA.
FEMS Immunol Med Microbiol. 1995 Jun;11(3):163-9. doi: 10.1111/j.1574-695X.1995.tb00113.x.
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.
本研究的目的是利用来自麻风病人的免疫球蛋白以及与溴化氰活化的琼脂糖凝胶4B偶联的兔抗麻风杆菌超免疫血清，通过免疫亲和层析法分离麻风杆菌抗原。分离出了一种高分子量（M(r)）的麻风杆菌蛋白（MLP），其亚基M(r)为22,000。MLP可被单克隆抗体MMPII1G4识别，已知该抗体可与麻风杆菌的一种22 kDa蛋白MMPII发生反应。22 kDa亚基的N端序列（Met-gln-gly-asp-pro-asp-val-leu-arg-leu-leu-asn-glu-gln-leu-thr）与MMPII以及副结核分枝杆菌的抗原D（细菌铁蛋白）相同。它与大肠杆菌细菌铁蛋白的N端显示出44%的同源性。在酶联免疫吸附测定（ELISA）中，与正常健康血清相比，MLP与麻风血清和结核血清的阳性反应率分别为100%和60%。本文讨论了细菌铁蛋白在麻风杆菌中的作用以及MLP作为免疫原的重要性。
