Activation of a RhoA/myosin II-dependent but Arp2/3 complex-independent pathway facilitates Salmonella invasion.

Salmonella stimulates host cell invasion using virulence effectors translocated by the pathogen's type-three secretion system (T3SS). These factors manipulate host signaling pathways, primarily driven by Rho family GTPases, which culminates in Arp2/3 complex-dependent activation of host actin nucleation to mediate the uptake of Salmonella into host cells. However, recent data argue for the existence of additional mechanisms that cooperate in T3SS-dependent Salmonella invasion. We identify a myosin II-mediated mechanism, operating independent of but complementary to the Arp2/3-dependent pathway, as contributing to Salmonella invasion into nonphagocytic cells. We also establish that the T3SS effector SopB constitutes an important regulator of this Rho/Rho kinase and myosin II-dependent invasion pathway. Thus, Salmonella enters nonphagocytic cells by manipulating the two core machineries of actin-based motility in the host: Arp2/3 complex-driven actin polymerization and actomyosin-mediated contractility.