Protein tyrosine phosphorylation in Mycobacterium tuberculosis.
Crude cell extracts from three strains of Mycobacterium tuberculosis were analyzed for the presence of proteins possessing phosphorylated tyrosine residues. A protein migrating at approximately 55 kDa was detected using an antiphosphotyrosine monoclonal antibody. In addition, less predominant bands were observed between 50 kDa and 60 kDa. That M. tuberculosis contains specific tyrosine phosphorylated proteins implies that M. tuberculosis has tyrosine kinase activity. Examination of other, non-pathogenic mycobacterium species yielded no major antiphosphotyrosine reactive proteins. This suggests that the antiphosphotyrosine reactive protein is specific to M. tuberculosis strains. These results provide evidence that M. tuberculosis contains an antiphosphotyrosine reactive protein.
Chow
K
K
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
Ng
D
D
Stokes
R
R
Johnson
P
P
D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D010766:Phosphorylation; D019000:Phosphotyrosine; D014443:Tyrosine / Q000031:analogs & derivatives / Q000032:analysis / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins; D019000:Phosphotyrosine; D014443:Tyrosine