Open AccessProtein tyrosine phosphorylation in Mycobacterium tuberculosis
Author(s) -
Chow Kevin,
Ng David,
Stokes Richard,
Johnson Pauline
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07285.x
Subject(s) - mycobacterium tuberculosis , tyrosine , phosphorylation , biology , monoclonal antibody , tyrosine phosphorylation , biochemistry , mycobacterium , tuberculosis , microbiology and biotechnology , bacteria , antibody , immunology , medicine , genetics , pathology
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.