[ODP-160] Leptospira interrogans induces decrease of proteins involved in junction stabilization
Leptospira interrogans disseminates hematogenously and reach the target organs, such as the kidney, lung and liver. We have recently demonstrated that L. interrogans induces E-cadherin endocytosis, cytoskeletal rearrangement, and mislocalization of tight junction proteins, resulting in apical junctional complex (AJC) disassembly for opening the paracellular route. In this study, we performed a proteomic analysis to understand the strategy used by Leptospira interrogans to dismantle the AJC. Human renal proximal tubule epithelial cells were infected during 4 h or 24 h with L. interrogans and infected cells were subjected to proteomic analysis by LC-MS/MS. A total of 6792 human proteins and 1190 leptospiral proteins were identified. Among them, 119 human proteins were significantly increased and 198 significantly decreased at 24 h post-infection. Two armadillo-repeat containing proteins (p0071 and p120-catenin) involved in junction stabilization through its binding to the E-cadherin juxtamembrane domain, were identified among the most decreased host proteins during infection. Analysis of p0071 by Western blotting and immunofluorescence showed a significant decreased of the protein at 24 h post-infection. Our results suggested that L. interrogans targets armadillo-repeat containing proteins involved in the stabilization of E-cadherin at the plasma membrane.