期刊
FEBS LETTERS
卷 591, 期 20, 页码 3276-3287出版社
WILEY
DOI: 10.1002/1873-3468.12848
关键词
bacteriophage; endolysin; mycobacteria
资金
- Council of Scientific and Industrial Research, Govt. of India
- Department of Science and Technology, Govt. of India [DST/INSPIRE Fellowship/2012/482]
- Department of Biotechnology, Govt. of India [BT/PR20257/BBE/117/223/2016, BT/PR8138/BID/7/458/2013]
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.
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