PtpA， a secreted tyrosine phosphatase from ， contributes to virulence and interacts with coronin-1A during infection.

Secretion of bacterial signaling proteins and adaptation to the host， especially during infection， are processes that are often linked in pathogenic bacteria. The human pathogen is equipped with a large arsenal of immune-modulating factors， allowing it to either subvert the host immune response or to create permissive niches for its survival. Recently， we showed that one of the low-molecular-weight protein tyrosine phosphatases produced by ， PtpA， is secreted during growth. Here， we report that deletion of in affects intramacrophage survival and infectivity. We also observed that PtpA is secreted during macrophage infection. Immunoprecipitation assays identified several host proteins as putative intracellular binding partners for PtpA， including coronin-1A， a cytoskeleton-associated protein that is implicated in a variety of cellular processes. Of note， we demonstrated that coronin-1A is phosphorylated on tyrosine residues upon infection and that its phosphorylation profile is linked to PtpA expression. Our results confirm that PtpA has a critical role during infection as a bacterial effector protein that counteracts host defenses.