New bioactive peptides from the venom gland of a social hornet Vespa velutina

Meng, Yichuan; Mo, Xianggui; He, Tiantian; Wen, Xinxin; Nieh, James C.; Yang, Xinwang; Tan, Ken

doi:10.1016/j.toxicon.2021.06.002

Cited by 10 publications

(4 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It would be interesting to conduct a broader study of the sequences of all the different venom AMPs that have antimicrobial effects. New data on mastoparan-like AMPs (U-VVTX-Vp1a, U-VVTX-Vp1b, U-VVTX-Vp2a, and U-VVTX-Vp2b) from the venom of V. velutina could help inform this effort (Meng et al, 2021). Peptides with similar sequences have been found in the venom of wasps such as Eumenes pomiformis and Orancistrocerus drewseni (Baek and Lee, 2010;Lee et al, 2016;Konno et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

“…AMPs in the mastoparan family have a wide range of applications and have shown promise in antibacterial and cancer therapies (Yamada et al, 2005;Moreno and Giralt, 2015;Silva et al, 2020). Recently, we reported on mastoparan-like AMPs (U-VVTX-Vp1a, U-VVTX-Vp1b, U-VVTX-Vp2a, and U-VVTX-Vp2b) from the venom of V. velutina (Meng et al, 2021). All four of these peptides showed scavenging ability against DPPH, ABTS + , and •OH free radicals.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis)

Wen

Gongpan

Meng

et al. 2021

Toxicon

Self Cite

View full text Add to dashboard Cite

Antibiotic-resistant bacteria are a major threat to global public health, and there is an urgent need to find effective, antimicrobial treatments that can be well tolerated by humans. Hornet venom is known to have antimicrobial properties, and contains peptides with similarity to known antimicrobial eptides (AMPs), mastoparans. We identified multiple new AMPs from the venom glands of Vespa ducalis (U-VVTX-Vm1a, U-VVTX-Vm1b, and U-VVTX-Vm1c), Vespa mandarinia (U-VVTX-Vm1d), and Vespa affinis (U-VVTX-Vm1e). All of these AMPs have highly similar sequences and are related to the toxic peptide, mastoparan. Our newly identified AMPs have α-helical structures, are amphiphilic, and have antimicrobial properties. Both U-VVTX-Vm1b and U-VVTX-Vm1e killed bacteria, Staphylococcus aureus ATCC25923 and Escherichia coli ATCC25922, at the concentrations of 16 μg/mL and 32 μg/mL, respectively. None of the five AMPs exhibited strong toxicity as measured via their hemolytic activity on red blood cells. U-VVTX-Vm1b was able to increase the permeability of E. coli ATCC25922 and degrade its genomic DNA. These results are promising, demonstrate the value of investigating hornet venom as an antimicrobial treatment, and add to the growing arsenal of such naturally derived treatments.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis)

Wen

Gongpan

Meng

et al. 2021

Toxicon

Self Cite

View full text Add to dashboard Cite

show abstract

“…The hemolytic activity of OA-GL17d was detected according to previous research [ 25 ]. Red blood cells were collected from Kunming mice ( n = 3), washed with saline three times, diluted with saline, then 0.1% TritonX-100 and OA-GL17d (0.1, 0.5, 1 mg/ml) were added and incubated in a 37°C water bath for 30 min.…”

Section: Methodsmentioning

confidence: 99%

Amphibian-derived peptide homodimer OA-GL17d promotes skin wound regeneration through the miR-663a/TGF-β1/Smad axis

et al. 2022

View full text Add to dashboard Cite

Background Amphibian-derived peptides exhibit considerable potential in the discovery and development of new therapeutic interventions for clinically challenging chronic skin wounds. MicroRNAs (miRNAs) are also considered promising targets for the development of effective therapies against skin wounds. However, further research in this field is anticipated. This study aims to identify and provide a new peptide drug candidate, as well as to explore the underlying miRNA mechanisms and possible miRNA drug target for skin wound healing. Methods A combination of Edman degradation, mass spectrometry and cDNA cloning were adopted to determine the amino acid sequence of a peptide that was fractionated from the secretion of Odorrana andersonii frog skin using gel-filtration and reversed-phase high-performance liquid chromatography. The toxicity of the peptide was evaluated by Calcein-AM/propidium iodide (PI) double staining against human keratinocytes (HaCaT cells), hemolytic activity against mice blood cells and acute toxicity against mice. The stability of the peptide in plasma was also evaluated. The prohealing potency of the peptide was determined by MTS, scratch healing and a Transwell experiment against HaCaT cells, full-thickness injury wounds and scald wounds in the dorsal skin of mice. miRNA transcriptome sequencing analysis, enzyme-linked immunosorbent assay, real-time polymerase chain reaction and western blotting were performed to explore the molecular mechanisms. Results A novel peptide homodimer (named OA-GL17d) that contains a disulfide bond between the 16th cysteine residue of the peptide monomer and the sequence ‘GLFKWHPRCGEEQSMWT’ was identified. Analysis showed that OA-GL17d exhibited no hemolytic activity or acute toxicity, but effectively promoted keratinocyte proliferation and migration and strongly stimulated the repair of full-thickness injury wounds and scald wounds in the dorsal skin of mice. Mechanistically, OA-GL17d decreased the level of miR-663a to increase the level of transforming growth factor-β1 (TGF-β1) and activate the subsequent TGF-β1/Smad signaling pathway, thereby resulting in accelerated skin wound re-epithelialization and granular tissue formation. Conclusions Our results suggest that OA-GL17d is a new peptide drug candidate for skin wound repair. This study emphasizes the importance of exogenous peptides as molecular probes for exploring competing endogenous RNA mechanisms and indicates that miR-663a may be an effective target for promoting skin repair.

show abstract

“…The active ingredients are mainly antimicrobe peptides (AMP). For example, coprisin [ 129 ], lebocin [ 148 ], drosocin [ 136 ], pronectin [ 143 ], cecropin [ 146 ], etc. Besides, certain unsaturated fatty acid [ 125 ], protein (e.g., lectin [ 130 ] and lysozyme [ 137 ], and terpenoid (e.g., cantharidin [ 128 ]) also showed antimicrobe/virus effects.…”

Section: Effects and Consequences Of Using Medicinal Insectsmentioning

confidence: 99%

Unravelling the potential of insects for medicinal purposes – A comprehensive review

Siddiqui

Aidoo³

et al. 2023

Heliyon

View full text Add to dashboard Cite

New bioactive peptides from the venom gland of a social hornet Vespa velutina

Cited by 10 publications

References 40 publications

Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis)

Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis)

Amphibian-derived peptide homodimer OA-GL17d promotes skin wound regeneration through the miR-663a/TGF-β1/Smad axis

Unravelling the potential of insects for medicinal purposes – A comprehensive review

Contact Info

Product

Resources

About