Characterization of the secreted antigens of Mycobacterium bovis BCG: comparison of the 46-kilodalton dimeric protein with proteins MPB64 and MPB70

Author:

Abou-Zeid C1,Harboe M1,Rook G A1

Affiliation:

1. Department of Microbiology, School of Pathology, Middlesex Hospital Medical School, London, United Kingdom.

Abstract

Western blot analysis showed that the 46-kilodalton (kDa) dimeric protein antigen secreted in large amounts by some daughter strains of Mycobacterium bovis BCG corresponded to protein MPB70 present in long-term culture filtrates of the Japanese substrain. The 46/23-kDa antigen is the most abundant protein in supernatant from a 5-day culture but is masked by leaked products in old culture supernatants. No similarities were found between the 46-kDa protein and MPB64, a protein with the same strain distribution, or with the antigen of similar molecular mass recognized by monoclonal antibody SA1.D2D.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference7 articles.

1. A simple new method for using antigens separated by polyacrylamide gel electrophoresis to stimulate Iymphocytes in vitro after converting bands cut from Western blots into antigen-bearing particles;Abou-Zeid C.;J. Immunol. Methods,1987

2. Subdivision of daughter strains of Bacille Calmette-Guerin (BCG) according to secreted protein patterns;Abou-Zeid C.;J. Gen. Microbiol.,1986

3. MPB 70, a unique antigen of Mycobacterium bovis BCG;Harboe M.;Am. Rev. Respir. Dis.,1984

4. Properties of proteins MPB64, MPB70, and MPB80 of Mycobacterium bovis BCG;Harboe M.;Infect. Immun.,1986

5. Comparative studies with various substrains of Mycobacterium bovis BCG on the production of an antigenic protein, MPB 70;Miura K.;Infect. Immun.,1983

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