Recruitment of LC3 by to Bacterial Invasion Site on Host Cells the Rac1-Mediated Signaling Pathway.

is a leading cause of food-borne disease worldwide. The pathogenicity of is closely associated with the internalization process in host epithelial cells, which is related to a host immune response. Autophagy indicates a key role in the innate immune system of the host to exclude invasive pathogens. Most bacteria are captured by autophagosomes and degraded by autophagosome-lysosome fusion in host cells. However, several pathogens, such as and , avoid and/or escape autophagic degradation to establish infection. But autophagy involvement as a host immune response to infection has not been clarified. This study revealed autophagy association in infection. During infection, activated the Rho family small GTPase Rac1 signaling pathway, which modulates actin remodeling and promotes the internalization of this pathogen. In this study, we found the LC3 contribution to invasion signaling the Rac1 signaling pathway. Interestingly, during invasion, LC3 was recruited to bacterial entry site depending on Rac1 GTPase activation just at the early step of the infection. infection induced LC3-II conversion, and autophagy induction facilitated internalization. Also, autophagy inhibition attenuated invasion step. Moreover, Rac1 recruited LC3 to the cellular membrane, activating the invasion of . Altogether, our findings provide insights into the new function of LC3 in bacterial invasion. We found the interaction between the Rho family small GTPase, Rac1, and autophagy-associated protein, LC3.