In Silico Characterization and Screening for Inhibitors of Sdia: A Protein Involved in Quorom Sensing in Escherichia Coli

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Bacteria use quorum sensing as a way of inter and intra- species communication. Quorum sensing was found to be important for bacteria for various processes including establishing an infection through virulence and biofilm formation. This is mediated autoinducers, which are usually produced by one group of bacteria and recognized by another group through a response regulator protein. LuxR is a response regulator protein first discovered in Vibreo fischeri and it recognizes autoinducers produced by the same species of bacteria. E. coli also has a response regulator called SdiA which is a homolog of LuxR, originally found to be involved in transcription and cell division. SdiA was later reported to regulate quorum sensing by binding to autoinducers called Acyl Homoserine Lactones (AHLs). SdiA is also reported to be involved in enhancing the multidrug resistance and virulence in pathogenic E. coli. Though many studies elaborate the functional aspects of SdiA, sequence and structural level analysis of this protein is missing in the literature. The current work aims at the in silico analysis and targeting of SdiA with structural analogs of AHLs. 7 compounds were found to be promising molecules to inhibit quorum sensing in E. coli.