Venom peptides from solitary hunting wasps induce feeding disorder in lepidopteran larvae
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| Title: | Venom peptides from solitary hunting wasps induce feeding disorder in lepidopteran larvae |
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| Authors: | Jeon Soo Shin, Si Hyeock Lee, Ji Hyeong Baek, Yeounjung Ji, Seunghwan Lee |
| Contributors: | Ji Hyeong Baek, Yeounjung Ji, Jeon-Soo Shin, Seunghwan Lee, Si Hyeock Lee, Shin, Jeon Soo |
| Source: | Peptides. 32:568-572 |
| Publisher Information: | Elsevier BV, 2011. |
| Publication Year: | 2011 |
| Subject Terms: | Hemolysis/drug effects, 0301 basic medicine, Peptides/pharmacology, Cell lysis, Cells, Wasps, Venoms/chemistry, Peptides/chemistry, Hemolysis, Anti-Bacterial Agents/pharmacology, 03 medical and health sciences, Venom peptide, Larva/drug effects, Animals, Humans, Feeding Behavior/drug effects, Cells, Cultured, Wasps/chemistry, 0303 health sciences, Cultured, Bacteria, Venoms, Fungi, Feeding Behavior, Lepidoptera/physiology, Anti-Bacterial Agents, 3. Good health, Lepidoptera, Lepidoptera/drug effects, Bacteria/drug effects, Larva, Solitary wasp, Larva/physiology, Antimicrobial peptide, Peptides, Fungi/drug effects |
| Description: | The cell lytic activity and toxicity against lepidopteran larvae of 13 venom peptides (4 OdVPs and 9 EpVPs) from two solitary hunting wasps, Orancistrocerus drewseni and Eumenes pomiformis, were examined with mastoparan as a reference peptide. Of the 13 peptides, 7 were predicted to have α-helical structures that exhibit the typical character of amphipathic α-helical antimicrobial peptides. The remaining peptides exhibited coil structures; among these, EpVP5 possesses two Cys residues that form an internal disulfide bridge. All the helical peptides including mastoparan showed antimicrobial and insect cell lytic activities, whereas only two of them were hemolytic against human erythrocytes. The helical peptides induced a feeding disorder when injected into the vicinity of the head and thorax of Spodoptera exigua larvae, perhaps because their non-specific neurotoxic or myotoxic action induced cell lysis. At low concentrations, however, these helical peptides increased cell permeability without inducing cell lysis. These findings suggest that the helical venom peptides may function as non-specific neurotoxins or myotoxins and venom-spreading factors at low concentrations, as well as preservatives for long-term storage of the prey via antimicrobial, particularly antifungal, activities. |
| Document Type: | Article |
| File Description: | 568~572 |
| Language: | English |
| ISSN: | 0196-9781 |
| DOI: | 10.1016/j.peptides.2010.12.007 |
| Access URL: | https://pubmed.ncbi.nlm.nih.gov/21184791 https://europepmc.org/abstract/MED/21184791 https://www.ncbi.nlm.nih.gov/pubmed/21184791 https://www.sciencedirect.com/science/article/pii/S0196978110005358 |
| Rights: | Elsevier TDM CC BY NC ND |
| Accession Number: | edsair.doi.dedup.....b98d263c93e6d8c6b88f8b1534a2c8e5 |
| Database: | OpenAIRE |
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Nájsť tento článok vo Web of Science | Abstract: | The cell lytic activity and toxicity against lepidopteran larvae of 13 venom peptides (4 OdVPs and 9 EpVPs) from two solitary hunting wasps, Orancistrocerus drewseni and Eumenes pomiformis, were examined with mastoparan as a reference peptide. Of the 13 peptides, 7 were predicted to have α-helical structures that exhibit the typical character of amphipathic α-helical antimicrobial peptides. The remaining peptides exhibited coil structures; among these, EpVP5 possesses two Cys residues that form an internal disulfide bridge. All the helical peptides including mastoparan showed antimicrobial and insect cell lytic activities, whereas only two of them were hemolytic against human erythrocytes. The helical peptides induced a feeding disorder when injected into the vicinity of the head and thorax of Spodoptera exigua larvae, perhaps because their non-specific neurotoxic or myotoxic action induced cell lysis. At low concentrations, however, these helical peptides increased cell permeability without inducing cell lysis. These findings suggest that the helical venom peptides may function as non-specific neurotoxins or myotoxins and venom-spreading factors at low concentrations, as well as preservatives for long-term storage of the prey via antimicrobial, particularly antifungal, activities. |
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| ISSN: | 01969781 |
| DOI: | 10.1016/j.peptides.2010.12.007 |