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I. Elucidation of TRP120, an Ehrlichial Type 1 Secreted Substrate as a Nucleomodulin.
II. Role of SsaP in Salmonella Pathogenicity Island-2 encoded Type 3 Secretion System
The study confirmed the role of the small protein, SsaP, in the secretion of the substrates via the Type 3 Secretion system (T3SS). We also showed that the mutant defective for SsaP exhibited poor intracellular replication in HeLa cells. Based on the homology with related proteins, it is likely the molecular ruler for the SPI-2 encoded T3SS. However the mechanism by which the small protein modulates the SPI-2 T3SS still remains to be elucidated.
III. Characterization of Sulfatases in Salmonella enterica serovar Typhimurium
My PhD dissertation addressed the characterization of a highly conserved gene family-sulfatases in Salmonella. I was investigating different environmental cues that regulate the expression of these enzymes. The study identified two novel sulfatase in Salmonella. One of them was under the control of OmpR~EnvZ two component system and expressed under mild acidic pH, which is encountered by the bacteria in the macrophages. Another sulfatase was expressed in the presence of monoamine compounds and was regulated by a LuxR type of transcriptional regulator. Interestingly these monoamine compounds are abundant in the gastrointestinal tract and also widespread in the plant kingdom. Their role in pathogenesis has been reported recently and thus inhibitors for the sulfatases might serve as potential therapeutic targets against Salmonella infections.
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