Title: Sortase A mediated peptide recruitment as a potential anti-virulence treatment for Staphylococcus aureus infection
Sortase A is a transpeptidase enzyme that is majorly present onto the cell wall of Gram-positive bacteria. It recognized and displays proteins on the cell wall via a conserved motif LPXTG at C- terminal. These proteins plays a major role in the virulence of the bacteria. Cell surface proteins not only helps bacteria to enter the host cells but also helps the bacteria to evade the immune systems using various mechanisms. In this study we have used a foreign peptide having LPETG motif at the C-terminal to redecorate the cell wall of the bacteria. Here, we used the approach to study the bacterial response after the recruitment of Foreign peptide onto the fibronectin binding, complement system activations and the pathogenesis of the bacteria. Here, we have observed a significant decrease in the binding of the Staphylococcus aureus to fibronectin by which bacteria enter in the host cells. As well as we have also observed a increase in the phagocytosis of the bacteria after the peptide treatment in-vitro. The present work provides a novel method to combat the Gram-positive infection by attenuating its virulence.