%A Nomaguchi H
%A Matsuoka M
%A Kohsaka K
%A Nakata A
%A Ito T
%T Overproduction, affinity purification and characterization of 65-kDa protein of Mycobacterium leprae in Escherichia coli
%0 Journal Article
%D 1989
%J International Journal of Leprosy and other Mycobacterial Diseases
%P 0148-916X
%V 57
%N 4
%X The 65-kDa protein of Mycobacterium leprae was produced in an Escherichia coli strain carrying a plasmid harboring the re-cloned gene coding for the protein. The protein was purified through affinity chromatography prepared with the IgG fraction of a monoclonal antibody which was prepared against the 65-kDa protein. The purified 65-kDa protein also reacted immunologically with the monoclonal antibody IIIE9, which recognizes the epitope for M. leprae, prepared by Buchanan, et al. BALB/c mice were inoculated with M. leprae and 4 months later were skin tested with the purified 65-kDa protein. Gross changes were observed at the skin-test site. The role of the protein in protective immunity against M. leprae foot pad infection in mice was also studied.