Overproduction, affinity purification and characterization of 65-kDa protein of Mycobacterium leprae in Escherichia coli.
The 65-kDa protein of Mycobacterium leprae was produced in an Escherichia coli strain carrying a plasmid harboring the recloned 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.
Nomaguchi
H
H
Research Institute for Microbial Diseases, Osaka University, Japan.
Matsuoka
M
M
Kohsaka
K
K
Nakata
A
A
Ito
T
T
D000818:Animals; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000276:immunology; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism*; D005260:Female; D006968:Hypersensitivity, Delayed; D051379:Mice; D008807:Mice, Inbred BALB C; D009166:Mycobacterium leprae / Q000276:immunology*
D001426:Bacterial Proteins