Investigations on the Interactions of λPhage-Derived Peptides Against the SrtA Mechanism in Bacillus anthracis
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Abstract
Bacillus anthracis is a well-known bioweapon pathogen, which coordinates the expression of its virulence factors in response to a specific environmental signal by its protein architecture. Absences of sortase signal functioning may fail to assemble the surface linked proteins and so B. anthracis cannot sustain an infection with host cells. Targeting the signaling mechanism of B. anthracis can be achieved by inhibition of SrtA enzyme through λphage-derived plyG. The lysin enzyme plyG is experimentally proven as bacteriolytic agent, specifically kill's B. anthracis by inhibiting the SrtA. Here, we have screened the peptides from λphage lysin, and these peptides are having the ability as LPXTG competitive inhibitors. In comparison to the activator peptide LPXTG binding motif, λphage lysin based inhibitor peptides are having much supremacy towards binding of SrtA. Finally, peptide structures extracted from PlyG are free from toxic, allergic abilities and also have the ability to terminate the signal transduction mechanism in B. anthracis.
Keywords
Activator LPXTG Peptide PlyG Peptidomimetic SrtANotes
Acknowledgments
The authors thankfully acknowledge the CSIR for research funding and fellowship grants (Ref. No: 37(1491)/11/EMR-II). One of the authors Chandrabose Selvaraj gratefully acknowledges CSIR for the Senior Research Fellowship (SRF). The authors thank anonymous referees for the valuable suggestion on this research work.
Conflict of Interests
None
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