ArticleMolecules (Basel, Switzerland)2016
MP-V1 from the Venom of Social Wasp Vespula vulgaris Is a de Novo Type of Mastoparan that Displays Superior Antimicrobial Activities.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 20 citations in OpenAlex.
- Entomophagy and entomo-therapeutic practices in a mountainous territory in southeast Guangxi Zhuang Autonomous Region, China.Journal of ethnobiology and ethnomedicine · 2024Article
- Mutualistic Relationships between Microorganisms and Eusocial Wasps (Hymenoptera, Vespidae).Microorganisms · 2023Review
- Article
- Bioactive Peptides and Proteins from Wasp Venoms.Biomolecules · 2022Review
- Mastoparans: A Group of Multifunctional α-Helical Peptides With Promising Therapeutic Properties.Frontiers in molecular biosciences · 2022Review
- Wasp Venom Biochemical Components and Their Potential in Biological Applications and Nanotechnological Interventions.Toxins · 2021Review
- Article
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Authors and funding
9 authors at 2 institutions in 1 country.
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Abstract
Mastoparans from the venom of social wasps have attracted considerable attention as effective antibiotic candidates. In this study, mastoparan V1 (MP-V1) from Vespula vulgaris was first disclosed to have a peptide amino acid sequence distinct from typical mastoparans and its biochemical properties and antimicrobial effects were compared with those of typical mastoparans MP-L, -X(V) and -B. Circular dichroism (CD) spectroscopy revealed that MP-V1 and -X(V) form more stable α-helical conformations in lipid membrane-like environments than MP-L and -B. In parallel, these two also showed more effective antimicrobial activities against the pathogens than did MP-L and -B. Although MP-V1 had a less stable α-helical conformation than MP-X(V), it showed stronger antimicrobial effects against Streptococcus mutans and Salmonella enterica than MP-X(V). In the meantime, analysis of hemolytic activity revealed a range of doses (~50 μM) that exhibited little potent cytotoxicity on human erythrocytes. Finally, the atypical MP-V1 peptide amino acid sequence provided important clues to understanding its antimicrobial mechanism from a structural perspective. Therefore, it has been concluded that MP-V1 is a de novo type of mastoparan with superior antimicrobial activities against both pathogenic bacteria and fungi, which may be useful in developing multipurpose antimicrobial drugs against infectious diseases.
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