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Identification of cell wall binding domains and repeats in Streptococcus pneumoniae phage endolysins: A molecular and

Tahsin Khan1, Shakhinur Islam Mondal1, Araf Mahmud1

  • 1Department of Genetic Engineering and Biotechnology, Shahjalal University of Science and Technology, Sylhet, Bangladesh.

Biochemistry and Biophysics Reports
|November 1, 2024
PubMed

Insights

Multidrug-resistant Streptococcus pneumoniae requires new treatments. This study analyzes pneumococcal phage endolysins, identifying novel therapeutic targets for combating this global health threat.

Area of Science:

  • Microbiology and Virology
  • Structural Biology
  • Drug Discovery

Background:

  • Streptococcus pneumoniae (pneumococcus) is a multidrug-resistant pathogen causing severe diseases like pneumonia and meningitis.
  • The World Health Organization prioritizes pneumococcus as a global health threat, necessitating urgent development of alternative therapies to antibiotics.
  • Bacteriophage-derived endolysins offer potential as antimicrobial agents due to their ability to degrade bacterial cell walls.

Purpose of the Study:

  • To screen Streptococcus pneumoniae phage genomes for endolysins.
  • To create a database of these endolysins for molecular modeling and diversity analysis.
  • To gain insights into the structural and functional characteristics of pneumococcal phage endolysins for potential therapeutic development.

Main Methods:

  • Screening of Streptococcus pneumoniae phage genomes to curate endolysins.
  • Categorization of 89 endolysins into eight groups based on enzymatically active (EAD) and cell wall binding domains (CBDs).
  • Construction of three-dimensional structures, sequence analysis, and molecular docking studies (with choline).

Main Results:

  • A database of 89 endolysins from 81 phage genomes was established and categorized.
  • Structural analysis revealed conserved catalytic and ion-binding residues in several endolysin groups.
  • A novel, previously unknown cell wall binding repeat was identified in Group II endolysins, confirmed by molecular docking.

Conclusions:

  • This study provides the first comprehensive molecular and diversity analysis of Streptococcus pneumoniae phage endolysins.
  • The identified endolysins, particularly Group II with its additional binding repeat, represent promising candidates for novel lysin-based therapeutics.
  • Findings support the potential of bacteriophage endolysins as a viable alternative strategy against multidrug-resistant pneumococcal infections.
Keywords:
Alternatives to antibioticsDrug resistanceEndolysinStreptococcus pneumoniae

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