Background
Type: Article

Identification and biochemical characterization of a new antibacterial and antifungal peptide derived from the insect Sphodromantis viridis

Journal: Biochemistry (Moscow) (00062979)Year: 2015/04/15Volume: 80Issue: 4Pages: 433 - 440
Zare-Zardini H.Taheri Kafrani A.a Ordooei M. Ebrahimi L. Tolueinia B. Soleimanizadeh M.
DOI:10.1134/S0006297915040069Language: English

Abstract

Antimicrobial peptides are members of the immune system that protect the host from infection. In this study, a potent and structurally novel antimicrobial peptide was isolated and characterized from praying mantis Sphodromantis viridis. This 14-amino acid peptide was purified by RP-HPLC. Tandem mass spectrometry was used for sequencing this peptide, and the results showed that the peptide belongs to the Mastoparan family. The peptide was named Mastoparan-S. Mastoparan-S demonstrated that it has antimicrobial activities against a broad spectrum of microorganisms (Gram-positive and Gram-negative bacteria and fungi), and it was found to be more potent than common antibiotics such as kanamycin. Mastoparan-S showed higher antimicrobial activity against Gram-negative bacteria compared to Gram-positive ones and fungi. The minimum inhibitory concentration (MIC) values of Mastoparan-S are 15.1-28.3 μg/ml for bacterial and 19.3-24.6 μg/ml for fungal pathogens. In addition, this newly described peptide showed low hemolytic activity against human red blood cells. The in vitro cytotoxicity of Mastoparan-S was also evaluated on monolayer of normal human cells (HeLa) by MTT assay, and the results illustrated that Mastoparan-S had significant cytotoxicity at concentrations higher than 40 μg/ml and had no any cytotoxicity at the MIC (≤30 μg/ml). The findings of the present study reveal that this newly described peptide can be introduced as an appropriate candidate for treatment of topical infection. © 2015 Pleiades Publishing, Ltd.


Author Keywords

antimicrobial peptidescytotoxicityhemolytic activityimmune systemSphodromantis viridisAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntifungal AgentsAntimicrobial Cationic PeptidesHeLa CellsHumansInsect ProteinsMantodeaMicrobial Sensitivity TestsMolecular Sequence DataPhylogenySequence Analysis, Protein

Other Keywords

Amino Acid SequenceAnimalsAnti-Bacterial AgentsAntifungal AgentsAntimicrobial Cationic PeptidesHeLa CellsHumansInsect ProteinsMantodeaMicrobial Sensitivity TestsMolecular Sequence DataPhylogenySequence Analysis, ProteinBacteria (microorganisms)FungiHexapodaMantis religiosaNegibacteriaPosibacteriaSphodromantis viridisantifungal agentantiinfective agentantimicrobial cationic peptideinsect proteinmastoparan S, Sphodromantis viridisanimalchemistryHeLa cell linehumanisolation and purificationmicrobial sensitivity testmolecular geneticssequence analysis