Ctriporin, a New Anti-Methicillin-Resistant Staphylococcus aureus Peptide from the Venom of the Scorpion Chaerilus tricostatus

Abstract

Antibiotic-resistant microbes, such as methicillin-resistant Staphylococcus aureus, seriously threaten human health. The outbreak of "superbugs" in recent years emphasizes once again the need for the development of new antimicrobial agents or resources. Antimicrobial peptides have an evident bactericidal effect against multidrug-resistant pathogens. In the present study, a new antimicrobial peptide, ctriporin, was cloned and characterized from the venom of the scorpion Chaerilus tricostatus, an animal which has not yet been explored for toxic peptide resources. The MICs of ctriporin against Staphylococcus aureus, Bacillus thuringiensis, Bacillus subtilis, Micrococcus luteus, and Candida albicans are 5 to 20 g/ml. Meanwhile, it MIC against clinical antibiotic-resistant bacterial strains is 10 g/ml. Furthermore, the potential for ctriporin to be used as a topical antibiotic for treating staphylococcal skin infections was investigated. External use of the peptide ctriporin dramatically decreased the bacterial counts and cured skin infections in mice. In addition, ctriporin demonstrates antimicrobial efficacy via the bactericidal mechanism of rapid cell lysis. Together, these results suggest the potential of developing ctriporin as a new topical antibiotic.

Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis

“…To date, approximately 40 cationic peptides have been identified from various species of scorpions [8]. Some of them display great potential for application to the treatment of infections caused by antibiotic-resistant bacteria [9,10].…”

Insights into Antimicrobial Peptides from Spiders and Scorpions

“…Stigmurin exhibited both antibacterial and antifungal activity with MICs ranging from 8.7 to 69.5 µM [45]. The MICs of ctriporin against C. albicans are 5 to 20 µg/ml [85]. …”

New Generation Antibiotics/Antibacterials: Deadly Arsenal for Disposal of Antibiotic Resistant Bacteria

“…The best known examples of α-helical AMPs are magainin, protegrin, cyclic indolicin and coiled indolicin [46]. β-sheet peptides are composed of at least two β-strands with disulfide bonds between these strands [47] Researchers have identified, cloned and characterized a novel antimicrobial peptide from the venom of the scorpion Chaerilus tricostatus and named it as ctriporin [58]. The mature peptide of ctriporin was composed of 19 amino acid residues and possessed amidated C terminus.…”

“…Finally, a standard Grampositive bacterium, S. aureus, as a model bacterial strain is chosen to further explore the antimicrobial mechanism of ctriporin. All research about Ctriporin indicate it as an effective promising antimicrobial agent which act via the bactericidal mechanism of the rapid cell lysis [58].…”