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Protein phosphorylation plays a key role in  Mycobacterium tuberculosis  (Mtb) physiology and pathogenesis. We have previously shown that a secreted protein tyrosine phosphatase, PtpA, is essential for Mtb inhibition of host macrophage acidification and maturation, and is a substrate of the protein tyrosine kinase, PtkA, encoded in the same operon. In this study, we constructed a ∆ ptkA  deletion mutant in Mtb and found that the mutant exhibited impaired intracellular survival in the THP-1 macrophage infection model, correlated with the strain’s inability to inhibit macrophage phagosome acidification. By contrast, the mutant displayed increased resistance to oxidative stress  in vitro . Proteomic and transcriptional analyses revealed upregulation of  ptpA , and increased secretion of TrxB2, in the Δ ptkA  mutant. Kinase and protein-protein interaction studies demonstrated that TrxB2 is a substrate of PtkA phosphorylation. Taken together these studies establish a central role for the  ptk A- ptp A operon in Mtb pathogenesis.

Protein tyrosine kinase, PtkA, is required for Mycobacterium tuberculosis growth in macrophages