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Antimicrobial Peptide with a Bent Helix Motif Identified in Parasitic Flatworm Mesocestoides corti

Tomislav Rončević1, Marco Gerdol2, Sabrina Pacor2

  • 1Department of Biology, Faculty of Science, University of Split, 21000 Split, Croatia.

International Journal of Molecular Sciences
|November 9, 2024
PubMed

Insights

Researchers discovered mesco-2, a novel antimicrobial peptide (AMP) from the parasite Mesocestoides corti. This potent peptide shows broad-spectrum antibacterial activity and a unique membrane-targeting mechanism, offering a promising new antibiotic alternative.

Area of Science:

  • Parasitology
  • Biochemistry
  • Molecular Biology

Background:

  • The rise of antibiotic resistance necessitates the discovery of novel antimicrobial agents.
  • Antimicrobial peptides (AMPs) are a promising class of therapeutics, but parasite-derived AMPs are largely unexplored.
  • Mesocestoides corti is a parasitic flatworm with potential for novel bioactive compound discovery.

Purpose of the Study:

  • To identify and characterize novel antimicrobial peptides from the parasitic flatworm Mesocestoides corti.
  • To evaluate the antibacterial activity and mechanism of action of the most promising candidate, mesco-2.
  • To elucidate the structural basis for mesco-2's antimicrobial function.

Main Methods:

  • Genome-wide mining to identify potential AMP precursors in Mesocestoides corti.
  • Chemical synthesis and comprehensive characterization of the mesco-2 peptide.
  • In vitro antibacterial assays against a panel of Gram-negative and Gram-positive bacteria.
  • Circular dichroism spectroscopy to study peptide secondary structure in different environments.
  • Structure prediction and molecular dynamics simulations to model peptide-membrane interactions.

Main Results:

  • Three novel AMP precursors (mesco-1, -2, -3) were identified, with mesco-2 showing significant potential.
  • Synthesized mesco-2 exhibited potent broad-spectrum antibacterial activity against E. coli, K. pneumoniae, A. baumannii, P. aeruginosa, and S. aureus.
  • Mechanistic studies revealed a membrane-disrupting mechanism, with mesco-2 selectively targeting anionic bacterial membranes.
  • Circular dichroism and simulations indicated mesco-2 adopts a bent helical conformation on anionic membranes, driven by a specific amino acid motif.

Conclusions:

  • Mesco-2 is a potent, broad-spectrum antimicrobial peptide derived from a parasitic flatworm.
  • Its selective membrane interaction and unique structural features make it a promising candidate for novel antibiotic development.
  • This study underscores the potential of parasite-derived molecules as sources of innovative antimicrobial agents.
Keywords:
antimicrobial peptidesbent helix conformationmembranolytic activity

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