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Updated: Feb 23, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Dissecting the structure-function relationship in lysozyme domain of mycobacteriophage D29-encoded peptidoglycan

Himanshu Joshi1, Surya P Seniya1, Venkatesan Suryanarayanan2

  • 1Microbiology and Molecular Biology Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Bhopal, India.

FEBS Letters
|September 14, 2017
PubMed

Insights

Mycobacteriophage D29 Lysin A’s lysozyme domain (LD) effectively breaks down bacterial peptidoglycan. This research identifies key residues for enhanced LD activity, supporting its potential as a broad-spectrum therapeutic agent.

Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Bacteriophages offer a promising avenue for combating drug-resistant bacteria, including Mycobacterium tuberculosis.
  • Mycobacteriophage D29 Lysin A has demonstrated antimycobacterial activity.
  • The lysozyme domain (LD) of Lysin A is a key component responsible for hydrolyzing bacterial cell walls.

Discussion:

  • This study details the characterization of the D29 Lysin A lysozyme domain (LD).
  • The LD exhibits potent peptidoglycan hydrolysis against both gram-positive and gram-negative bacteria.
  • Identification of critical residues influencing LD activity and stability was achieved through extensive variant library analysis.

Key Insights:

  • The lysozyme domain (LD) of D29 Lysin A is a potent enzyme capable of degrading peptidoglycan in a broad range of bacteria.
  • Specific amino acid residues crucial for the LD's enzymatic activity and structural integrity have been identified.
  • In silico methods were employed to complement in vitro findings, providing a comprehensive understanding of LD function.

Outlook:

  • The characterized LD presents a strong candidate for the development of novel, phage-based, broad-spectrum antibacterial therapeutics.
  • Further research could focus on optimizing LD variants for enhanced efficacy and stability in therapeutic applications.
  • The findings contribute to the growing field of phage-derived antimicrobials as an alternative to conventional antibiotics.
Keywords:
bacteriophageendolysinmycobacteria

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