Biofilm-disrupting effects of phage endolysins LysAm24, LysAp22, LysECD7, and LysSi3: breakdown the matrix

World J Microbiol Biotechnol. 2024 Apr 29;40(6):186. doi: 10.1007/s11274-024-03999-9.

Abstract

The ability of most opportunistic bacteria to form biofilms, coupled with antimicrobial resistance, hinder the efforts to control widespread infections, resulting in high risks of negative outcomes and economic costs. Endolysins are promising compounds that efficiently combat bacteria, including multidrug-resistant strains and biofilms, without a low probability of subsequent emergence of stable endolysin-resistant phenotypes. However, the details of antibiofilm effects of these enzymes are poorly understood. To elucidate the interactions of bacteriophage endolysins LysAm24, LysAp22, LysECD7, and LysSi3 with bacterial films formed by Gram-negative species, we estimated their composition and assessed the endolysins' effects on the most abundant exopolymers in vitro. The obtained data suggests a pronounced efficiency of these lysins against biofilms with high (Klebsiella pneumoniae) and low (Acinetobacter baumannii) matrix contents, or dual-species biofilms, resulting in at least a twofold loss of the biomass. These peptidoglycan hydrolases interacted diversely with protective compounds of biofilms such as extracellular DNA and polyanionic carbohydrates, indicating a spectrum of biofilm-disrupting effects for bacteriolytic phage enzymes. Specifically, we detected disruption of acid exopolysaccharides by LysAp22, strong DNA-binding capacity of LysAm24, both of these interactions for LysECD7, and neither of them for LysSi3.

Keywords: Antibiofilm activity; Biofilm; Endolysin; Exopolysaccharides; Extracellular DNA.

MeSH terms

  • Acinetobacter baumannii / drug effects
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Bacteriophages* / enzymology
  • Biofilms* / drug effects
  • Biofilms* / growth & development
  • Endopeptidases* / chemistry
  • Endopeptidases* / metabolism
  • Endopeptidases* / pharmacology
  • Klebsiella pneumoniae / drug effects
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism
  • Viral Proteins / metabolism

Substances

  • Endopeptidases
  • endolysin
  • Viral Proteins
  • Anti-Bacterial Agents
  • N-Acetylmuramoyl-L-alanine Amidase