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Summary    S   almonella enterica   T yphimurium induces intestinal inflammation through the activity of type  III  secreted effector ( T3SE ) proteins. Our prior results indicate that the secretion of the  T3SE SipA  and the ability of  SipA  to induce epithelial cell responses that lead to induction of polymorphonuclear transepithelial migration are not coupled to its direct delivery into epithelial cells from   S   almonella . We therefore tested the hypothesis that  SipA  interacts with a membrane protein located at the apical surface of intestinal epithelial cells. Employing a split ubiquitin yeast‐two‐hybrid screen, we identified the tetraspanning membrane protein, p53 effector related to  PMP ‐22 ( PERP ), as a  SipA  binding partner.  SipA  and  PERP  appear to have intersecting activities as we found  PERP  to be involved in proinflammatory pathways shown to be regulated by  SipA . In sum, our studies reveal a critical role for  PERP  in the pathogenesis of   S  .  T yphimurium, and for the first time demonstrate that  SipA , a  T3SE  protein, can engage a host protein at the epithelial surface.

PERP, a host tetraspanning membrane protein, is required for S almonella ‐induced inflammation