Title |
The antimicrobial potential of a new derivative of cathelicidin from Bungarus fasciatus against methicillin-resistant Staphylococcus aureus |
Author |
Mercedeh Tajbakhsh1, Abdollah Karimi1, Abolghasem Tohidpour2, Naser Abbasi3,4, Fatemeh Fallah1, and Maziar Mohammad Akhavan5,6* |
Address |
1Pediatric Infections Research Center (PIRC), Research Institute for Children health, Shahid Beheshti University of Medical Sciences, Tehran, Iran, 2Research Institute of Molecular Medicine and Pathobiochemistry, Krasnoyarsk State Medical University, Krasnoyarsk, Russia, 3Department of Pharmacology, Faculty of Medicine, Ilam University of Medical Sciences, Ilam, Iran, 4Biotechnology and Medicinal Plants Research Center, Ilam University of Medical Sciences, Ilam, Iran, 5Skin Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran, 6Department of Pharmacology, Medical School, Iran University of Medical Sciences, Tehran, Iran |
Bibliography |
Journal of Microbiology, 56(2),128–137, 2018,
|
DOI |
10.1007/s12275-018-7444-5
|
Key Words |
antibiotic resistance, antimicrobial peptides, Cathelicidin-
BF, cytotoxic activity, MRSA |
Abstract |
Cathelicidins are a family of antimicrobial peptides which exhibit
broad antimicrobial activities against antibiotic-resistant
bacteria. Considering the progressive antibiotic resistance,
cathelicidin is a candidate for use as an alternative approach
to treat and overcome the challenge of antimicrobial resistance.
Cathelicidin-BF (Cath-BF) is a short antimicrobial peptide,
which was originally extracted from the venom of Bungarus
fasciatus. Recent studies have reported that Cath-BF and some
related derivatives exert strong antimicrobial and weak hemolytic
properties. This study investigates the bactericidal
and cytotoxic effects of Cath-BF and its analogs (Cath-A and
Cath-B). Cath-A and Cath-B were designed to increase their
net positive charge, to have more activity against methicillin
resistant S. aureus (MRSA). The results of this study show
that Cath-A, with a +17-net charge, has the most noteworthy
antimicrobial activity against MRSA strains, with minimum
inhibitory concentration (MIC) ranging between 32–128
μg/ml. The bacterial kinetic analysis by 1 × MIC concentration
of each peptide shows that Cath-A neutralizes the clinical
MRSA isolate for 60 min. The present data support the
notion that increasing the positive net charge of antimicrobial
peptides can increase their potential antimicrobial activity.
Cath-A also displayed the weakest cytotoxicity effect
against human umbilical vein endothelial and H9c2 rat cardiomyoblast
cell lines. Analysis of the hemolytic activity reveals
that all three peptides exhibit minor hemolytic activity
against human erythrocytes at concentrations up to 250 μg/ml.
Altogether, these results suggest that Cath-A and Cath-B are
competent candidates as novel antimicrobial compounds
against MRSA and possibly other multidrug resistant bacteria. |