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Background  Activation of inflammasome contributes to the clearance of intracellular bacteria. C-terminus of  E. coli  EscI protein can activate NLRC4 (NLR family, CARD domain containing-4) inflammasome in macrophages. The purpose of this study was to determine if activation of NLRC4 inflammasome by EscI can reduce the colonization of  Salmonella  in mice.    Results  A recombinant  S. typhimurium  strain expressing fusion protein of the N-terminal SspH2 (a  Salmonella  type III secretion system 2 effector) and C-terminal EscI was constructed and designated as X4550(pYA3334-SspH2-EscI). In vitro assay showed that X4550(pYA3334-SspH2-EscI) significantly enhanced IL-1β and IL-18 secretion ( P  < 0.05) and pyroptotic cell death of mouse peritoneal macrophages, compared with those infected with control strain, X4550(pYA3334-SspH2). In vivo studies showed that colonization of X4550(pYA3334-SspH2-EscI) in both spleen and liver were significantly lower than that of X4550(pYA3334-SspH2) ( P  < 0.05). The bacterial counts of X4550(pYA3334-SspH2-EscI) in mice decreased, while those of X4550(pYA3334-SspH2) increased over the time after infection. Additionally, X4550(pYA3334-SspH2-EscI) induced a less pathological alteration in spleen and liver than X4550(pYA3334-SspH2).    Conclusion  Fusion protein SspH2-EscI may be translocated into macrophages and activate NLRC4 inflammasome, which limits  Salmonella  colonization in spleen and liver of mice.

Recombinant Salmonella expressing SspH2-EscI fusion protein limits its colonization in mice