Dissecting the structure–function relationship in lysozyme domain of mycobacteriophage D29‐encoded peptidoglycan hydrolase. Issue 20 (20th September 2017)

• Record Type: Journal Article
• Authors: Joshi, Himanshu; Seniya, Surya P.; Suryanarayanan, Venkatesan; Patidar, Neelam D.; Singh, Sanjeev K.; Jain, Vikas
• Is Part Of: FEBS letters. Volume 591:Issue 20(2017)
• Page Start: 3276
• Page End: 3287
• Publication Date: 2017-09-20
• Subjects: bacteriophage -- endolysin -- mycobacteria; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12848
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract :