Mechanism of Bacteriophage Lytic Enzyme in Phage Therapy against Streptococcal Infection by in Silico Approach

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DOI: 10.21522/TIJCR.2014.04.02.Art009

Authors : Chethan Kumar S, VinodKumar C.S

Abstract:

Lysins or Lytic enzymes of Bacteriophage are highly evolved molecules produced to release their progeny by hydrolyzing the bacterial host cell wall. Now days, due to Multi Drug Resistance in many streptococcal infections; this mechanism is exploited as an alternative therapy against traditional antibiotic therapy. But in the treatment of phage therapy the mode of action is still unclear in the literatures. This study will evidence the probable mode of mechanism by the lysin in the breakage of host cell wall by In Silico approach. 3-D structure of Lysin was retrieved from Protein Data Bank and structure of peptidoglycan is retrieved from the PubChem. Docking studies was performed using Hex 6.3 taking lysin as receptor and peptidoglycan as ligand. Results were visualized in PyMol molecular visualization software. Docking studies showed the hydrophilic interaction between the peptidoglycan and lysin. The interacting residue of lysin belongs to CHAP domain which is responsible for the amidase catalytic activity which results in the breakage of cell wall for the release of their progeny. Molecular interactions between the lysin and peptidoglycan showed the possible mechanism for lysin which is responsible for breaking the major bonds in peptidoglycan layer for the release of bacteriophage progeny inside the host bacterial cell. This study will give the further evidence for the mode of action and by understanding this mechanism further improved therapies can be achieved in the Multi Drug Resistance bacterial infections.

Keywords: Bacteriophage, Streptococcus spp, Multi Drug Resistance bacterial infections, Lysin, Peptidoglycan, Docking studies.

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