4.4 Article

Identification and characterization of a novel antimicrobial peptide from the venom of the ant Tetramorium bicarinatum

Journal

PEPTIDES
Volume 38, Issue 2, Pages 363-370

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2012.08.018

Keywords

Tetramorium bicarinatum; Ant venom; Staphylococcus; ESI-MS/MS; Antibacterial peptide; AMP; Bicarinalin

Funding

  1. Region Midi-Pyrenees (France)
  2. University Champollion
  3. Urban Community of Albi (France)
  4. Agence Nationale de la Recherche (CEBA) [ANR-10-LABX-0025]

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A novel antimicrobial peptide, named Bicarinalin, has been isolated from the venom of the ant Tetramorium bicarinatum. Its amino acid sequence has been determined by de novo sequencing using mass spectrometry and by Edman degradation. Bicarinalin contained 20 amino acid residues and was C-terminally amidated as the majority of antimicrobial peptides isolated to date from insect venoms. Interestingly, this peptide had a linear structure and exhibited no meaningful similarity with any known peptides. Antibacterial activities against Staphylococcus aureus and S. xylosus strains were evaluated using a synthetic replicate. Bicarinalin had a potent and broad antibacterial activity of the same magnitude as Melittin and other hymenopteran antimicrobial peptides such as Pilosulin or Defensin. Moreover, this antimicrobial peptide has a weak hemolytic activity compared to Melittin on erythrocytes, suggesting potential for development into an anti-infective agent for use against emerging antibiotic-resistant pathogens. (C) 2012 Elsevier Inc. All rights reserved.

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