Antimicrobial peptides from the venoms of Vespa bicolor Fabricius

Chen, Wenhu; Yang, Xinbo; Yang, Xiaolong; Zhai, Lei; Lu, Zhenwu; Liu, Jingze; Yu, Haining

doi:10.1016/j.peptides.2008.07.018

Cited by 47 publications

(24 citation statements)

References 31 publications

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“…The toxin of V. crabro demonstrates bacteriostatic properties, especially the mastoparan contained in their venom. These properties have been found in toxins of many species of insects (Stocker & Traynor 1986, Yibin et al 2005, Xu et al 2006, Chen et al 2008.…”

Section: Accompanying Microorganisms In Wasp Nestsmentioning

confidence: 95%

Factors restricting the abundance of wasp colonies of the European hornet Vespa crabro and the Saxon wasp Dolichovespula saxonica (Hymenoptera: Vespidae) in an urban area in Poland

Nadolski¹

2013

Entomol. Fennica

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Various factors affecting the reproductive success of Vespacrabro and Dolichovespula saxonica (Vespinae), including their parasitoids, parasites, pathogens and other micro organisms accompanying their nests in the city of Lódz in Poland were investigated. Sphecophaga vesparum, Aphomia sociella and especially Quedius brevicornis, whose larvae cause destruction of wasp nests, were recorded. Totally 19 species or groups of bacteria, including pathogens like Pseudomon aeruginosa, Enterobacter cloacae, Staphylococcus aureus and Enterococcus faecalis, and 5 species of fungi were identified. Cities create very good conditions for wasp societies. Unfortunately, their presence can cause specific but important risks to humans, which lead to massive destruction of wasp nests. However, this does not cause considerable decrease in the number of colonies of common wasp species but less abundant species may be endangered in cities by this practice. It is thus recommended to limit the number of all wasp nests destroyed and to discriminate between the species.

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Section: Accompanying Microorganisms In Wasp Nestsmentioning

confidence: 95%

Factors restricting the abundance of wasp colonies of the European hornet Vespa crabro and the Saxon wasp Dolichovespula saxonica (Hymenoptera: Vespidae) in an urban area in Poland

Nadolski¹

2013

Entomol. Fennica

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“…Two families of bioactive peptides which belongs to mastoparans (12a and 12b) and chemotactic peptides (5e, 5g and 5f) were purified and characterized from the venom of Vespa magnifica. MP-VBs (vespa mastoparan) and VESP-VBs (vespa chemotactic peptide) were purified from the venom of the wasp Vespa bicolor Fabricius and demonstrated antimicrobial action [198]. The amphipathic α-helical structure and net positive charge (which permits electrostatic interaction with the negatively charged microbial cell membrane) of mastoparan appear to be critical for MCD activity and because of these structural properties, mastoparans are often highly active against the cell membranes of bacteria, fungi, and erythrocytes, as well as mast cells [199].…”

Section: Toxins With Antibiotic Activitymentioning

confidence: 99%

“…Echis carinatus EcTx-I Anti-bacterial agent [51] Naja atra Vgf-1 Anti-bacterial agent [54] Naja naja oxiana LAAO Anti-bacterial agent [46] Porthidium nasutum PnPLA 2 Anti-bacterial agent [52] Trimeresurus jerdonii TJ-LAO Anti-bacterial agent [41] Trimeresurus mucrosquamatus TM-LAO Anti-bacterial agent [43] Scorpions Hadrurus aztecus Hadrurin Anti-bacterial agent [110] Leiurus quinquestriatus Defensin Anti-bacterial agent [102] Opistophthalmus carinatus Opistoporin I/II Anti-bacterial and antifungal agent [106] Pandinus imperator Pandinin I/II Antimicrobial agent [101] Scorpine Anti-bacterial and antiparasitic agent [104] Parabuthus schlechteri Cationic amphipatic peptide Antimicrobial agent [109] Tityus discrepans Bactridines Anti-bacterial agent [111] Spiders Lycosa carolinensis Lycotoxins I/II Antimicrobial agent [150] Toads and Frogs Bufo bufo gargarizans 6-methylspinaceamine Anti-bacterial agent [172] Bufalin Antiviral agent [173] Cinobufagin Antiviral agent [173] Bufo rubescens Telocinobufagin Anti-bacterial agent [170] Marinobufagin Anti-bacterial agent [170] Leptodactylus pentadactylus Apinaceamine Anti-bacterial agent [172] Leptodactylus syphax SPXs Anti-bacterial agent [171] Rhinella jimi Telocinobufagin Antiparasitic agent [174] Hellebrigenin Antiparasitic agent [174] Bees and Wasps Apis mellifera Melittin Anti-bacterial agent [195] Bombus ignites Bi-Bombolitin Anti-bacterial and antifungal agent [196] Osmia rufa Osmin Anti-bacterial and antifungal agent [197] Vespa bicolor MP-VB1 Anti-bacterial and antifungal agent [198] VESP-VB1 Anti-bacterial and antifungal agent [198] Ants, Centipedes Sol i I Allergen [244] Sol i II Allergen [243] Sol i III Allergen [243] Sol i IV Allergen…”

Section: Toxins With Insecticides Applicationsmentioning

confidence: 99%

Toxins from Venomous Animals: Gene Cloning, Protein Expression and Biotechnological Applications

Fernandes-Pedrosa¹,

Félix-Silva²,

Menezes³

2013

An Integrated View of the Molecular Recognition and Toxinology - From Analytical Procedures to Biomedical Applications

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and binding site on different channels or channel subtypes. The venom is constituted by mucopolysaccharides, hyaluronidases, phospholipases, serotonins, histamines, enzyme inhibitors, antimicrobials and proteins namely neurotoxic peptides. Scorpion peptides presents specificity and high affinity and have been used as pharmacological tools to characterize various receptor proteins involved in normal ion channel functionating, as abnormal channel functionating in cases of diseases. The venoms can be characterized by identification of peptide toxins analysis of the structure of the toxins and also have proven to be among the most and selective antagonists available for voltage-gated channels permeable to K + , Na + , and Ca 2+. The neurotoxic peptides and small proteins lead to dysfunction and provoke pathophysiological actions, such as membrane destabilization, blocking of the central, and peripheral nervous systems or alteration of smooth or skeletal muscle activity [5-8]. Spider venoms are complex mixtures of biologically active compounds of different chemical nature, from salts to peptides and proteins. Specificity of action of some spider toxins is unique along with high toxicity for insects, they can be absolutely harmless for members of other taxons, and this could be essential for investigation of insecticides. Several spider toxins have been identified and characterized biochemically. These include mainly ribonucleotide phosphohydrolase, hyaluronidases, serine proteases, metalloproteases, insecticidal peptides and phospholipases D [9-10]. Venoms from toads and frogs have been extensively isolated and characterized showing molecules endowed with antimicrobial and/or cytotoxic activities [11]. Studies involving the molecular repertoire of the venom of bees and wasps have revealed the partial isolation, characterization and biological activity assays of histamines, dopamines, kinins, phospholipases and hyaluronidases. The venom of caterpillars has been partially characterized and contains mainly ester hydrolases, phospholipases and proteases [12]. The purpose of this chapter is to present the main toxins isolated and characterized from the venom of venomous animals, focusing on their biotechnological and pharmacological applications. 2. Biotechnological and pharmacological applications of snake venom toxins While the initial interest in snake venom research was to understand how to combat effects of snakebites in humans and to elucidate toxins mechanisms, snake venoms have become a fertile area for the discovery of novel products with biotechnological and/or pharmacological applications [13-14]. Since then, many different products have been developed based on purified toxins from snake venoms, as well recent studies have been showing new potential molecules for a variety of applications [15]. 2.1. Toxins acting on cardiovascular system Increase in blood pressure is often a transient physiological response to stressful stimuli, which allows the body to react to dangers or to promptly increase activity. However,...

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“…Mastoparan B, a cationic tetradecapeptide isolated from the venom of black-bellied hornet, Vespa basalis, the most dangerous species of vespine wasps found in Taiwan [1]. Mostoparan B exhibit several biological activities including mast cell degranulation and release of histamine [2], [3], hemolysis [2], [3], activation of phospholipase A2 [4], [5], phospholipase C [5], G proteins [6], and antibacterial activity. Unlike other vespid mastoparan toxins, mastoparan B more hydrophilic amino acid residues and was capable of inducing short-term hypotension in rats [7]- [10].…”

Section: Introductionmentioning

confidence: 99%

Cost-Effective Expression and Purification of Recombinant Venom Peptide Mastoparan B of Vespa Basalis in Escherichia Coli

Peng¹,

Hong²,

Tu³

2012

IJBBB

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Mastoparan B is a cationic, amphiphilic tetradecapeptide toxin isolated from the venom of the black-bellied hornet (Vespa basalis), the most dangerous species of wasps found in Taiwan. Mastoparan B was evaluate possess antibacterial activity and cardiovascular depress activity. However, mastoparan B is low abundance in the venom (3.4% of crude venom). In this study, mastoparan B was overexpressed in Escherichia coli BL21 as a recombinant protein fused the C-terminus of oleosin by a linker polypeptide, intein S. Artifical oil bodies (AOBs) were reconstituted with triacylglycerol, phospholipid to obtain the insoluble recombinant protein. Mastoparan B was subsequently released through self-splicing of intein induced by temperature alteration from artifical oli bodies, and the recombinant mastoparan B was collected it in the supernatant after centrifugation. Recombinant mastoparan B release from AOBs was exhibited membrane permeabilization activity, bacteriostatic and bactericidal activity. These results have shown that mastoparan B was successfully expressed and purified via the efficient AOB expression/purification system.

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Antimicrobial peptides from the venoms of Vespa bicolor Fabricius

Cited by 47 publications

References 31 publications

Factors restricting the abundance of wasp colonies of the European hornet <i>Vespa crabro</i> and the Saxon wasp <i>Dolichovespula saxonica</i> (Hymenoptera: Vespidae) in an urban area in Poland

Factors restricting the abundance of wasp colonies of the European hornet <i>Vespa crabro</i> and the Saxon wasp <i>Dolichovespula saxonica</i> (Hymenoptera: Vespidae) in an urban area in Poland

Toxins from Venomous Animals: Gene Cloning, Protein Expression and Biotechnological Applications

Cost-Effective Expression and Purification of Recombinant Venom Peptide Mastoparan B of Vespa Basalis in Escherichia Coli

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