Abstract

Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties.

Highlights

  • Antimicrobial peptides are widely found in plants, insects, amphibians, and mammals, playing an important role in innate immune systems and host defense mechanisms [1,2]

  • Eumenine mastoparan-AF (EMP-AF) was the first antimicrobial α-helical peptide that we found in the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado in the year 2000 [8]

  • Our studies on solitary wasps surveying bioactive components in their venoms revealed that antimicrobial peptides are contained in many wasp venoms, mostly in eumenine wasp venoms

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Summary

Introduction

Antimicrobial peptides are widely found in plants, insects, amphibians, and mammals, playing an important role in innate immune systems and host defense mechanisms [1,2]. The biological activities of these peptides may be due to the adoption of an amphipathic α-helical secondary structure that inserts into the lipids of biological membranes These peptides were tested in artificial lipid bilayers, and the channel-like activity observed demonstrated that ion conduction through biological membranes must be important to their lytic activity against mammal cells, but more importantly, against microorganisms [10,12,14,15,16]. This review summarizes these results from the studies on antimicrobial α-helical peptides in solitary wasp venoms. An overview of peptide toxins in solitary wasp venoms was summarized previously [17]

Chemical and Biological Characterization
Mastoparans
Eumenitins
Protonectin
Decoralin
Anoplin
Physicochemical Properties and Secondary Structure
Sequence and Chain Length
N- and C-Termini
Charge and Helix Macro-Dipole
Helical Propensity and Helicity
Amphipathicity and Hydrophobic Moment
Channel-Like Pore-Forming Properties
Eumenitin
Eumenitin-F and Eumenitin-R
EMP-EF and EMP-ER
Representative recordings of of single solitary wasp venom peptides
Findings
Concluding Remarks

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