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Dissecting the structure–function relationship in lysozyme domain of mycobacteriophage D29‐encoded peptidoglycan hydrolase
Author(s) -
Joshi Himanshu,
Seniya Surya P.,
Suryanarayanan Venkatesan,
Patidar Neelam D.,
Singh Sanjeev K.,
Jain Vikas
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12848
Subject(s) - lysin , peptidoglycan , biology , lysozyme , microbiology and biotechnology , lytic cycle , bacteriophage , in silico , bacteria , mycobacterium tuberculosis , biochemistry , escherichia coli , virology , genetics , gene , medicine , tuberculosis , virus , pathology
Most bacteriophages rapidly infect and kill bacteria and, therefore, qualify as the next generation therapeutics for rapidly emerging drug‐resistant bacteria such as Mycobacterium tuberculosis . We have previously characterized the mycobacteriophage D29‐generated endolysin, Lysin A, for its activity against mycobacteria. Here, we present a detailed characterization of the lysozyme domain ( LD ) of D29 Lysin A that hydrolyzes peptidoglycan of both gram‐positive and gram‐negative bacteria with high potency. By characterizing an exhaustive LD protein variant library, we have identified critical residues important for LD activity and stability. We further complement our in vitro experiments with detailed in silico investigations. We present LD as a potent candidate for developing phage‐based broad‐spectrum therapeutics.