The venom of the wasp Campsomeris Sexmaculata (F.) blocks synaptic transmission in insect cns

Piek, T.; Hue, Bernard; Pelhate, M.; Mony, Luc

doi:10.1016/0742-8413(87)90009-0

Cited by 7 publications

(6 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this study an uncommon type of wasp kinin was described because the peptide RA-Thr6-Bradykinin-DT contains both the dipeptide RA attached to the N-terminal residue of Thr6-Bradykinin, and the dipeptide DT attached to the C-terminal residue of this peptide. This wasp kinin type was previously reported in Megascolia flavifrons solitary wasp venom (Piek et al, 1987a(Piek et al, , 1987b, named as megascoliakinin (Thr6-BK-Lys-Ala), as well as in the Vespa analis (Nakajima, 1986).…”

Section: Kinin-related Peptidessupporting

confidence: 64%

“…Most of the kinin-related peptides in animal venoms have longer peptide chains and their actions are longer-lasting than BK (Piek, 1991). Thr 6 -Bradykinin is a neurotoxic component that has already been reported in the venom of solitary wasps M. flavifrons and Colpa interrupta (Piek et al, 1987a(Piek et al, , 1987b. According to literature, almost all social wasp venoms may have kinin or kinin-like activities, while among solitary wasps, Cyphononyx dorsalis (Pompilidae) and several Scoliidae wasps have Thr6-bradykinin in their venom; and bradykinin was found only in the Megacampsomeris prismatica (Scoliidae) venom (Konno et al, 2002).…”

Section: Kinin-related Peptidesmentioning

confidence: 97%

“…Other peptides similar to ponericins were also sequenced from Neoponera apicalis and Neoponera inversa ant venoms (Touchard et al, 2016a), showing a strong homology to the "G", "W" and "L" ponericin family. Recently, Pluzhnikov et al (2014) isolated three novel antimicrobial linear peptides (molecular weight 3 kDa), with homology to ponericin W5 peptides from Ectatomma brunneum ant venom (Pluzhnikov et al, 2014). These peptides showed antimicrobial and cytolytic activities at low micromolar concentrations.…”

Section: Cytolytic Peptidesmentioning

confidence: 99%

“…This peptide was shown to be a calcium channel blocker (Ca 2þ ), besides acting as a cytotoxic peptide in the formation of pores in vertebrate and invertebrate cells (Arseniev et al, 1994;Pluzhnikov et al, 1999). A homologue toxin, ectatomin Et-2 was further isolated from the ant venom (Pluzhnikov et al, 2014) Et-1 appears to account for the major toxic effect from Ectatomma tuberculatum venom, causing toxic effects in both mammals and insects (Pluzhnikov et al, 1999). These peptides are highly basic heterodimeric complexes and comprise two highly homologous amphiphilic polypeptide chains linked together by one inter-chain disulfide bond (Arseniev et al, 1994).…”

Section: Neurotoxic Peptidesmentioning

confidence: 99%

See 3 more Smart Citations

Diversity of peptidic and proteinaceous toxins from social Hymenoptera venoms

Santos-Pinto

Pérez-Riverol

Lasa

et al. 2018

Toxicon

View full text Add to dashboard Cite

Among venomous animals, Hymenoptera have been suggested as a rich source of natural toxins. Due to their broad ecological diversity, venom from Hymenoptera insects (bees, wasps and ants) have evolved differentially thus widening the types and biological functions of their components. To date, insect toxinology analysis have scarcely uncovered the complex composition of bee, wasp and ant venoms which include low molecular weight compounds, highly abundant peptides and proteins, including several allergens. In Hymenoptera, these complex mixtures of toxins represent a potent arsenal of biological weapons that are used for self-defense, to repel intruders and to capture prey. Consequently, Hymenoptera venom components have a broad range of pharmacological targets and have been extensively studied, as promising sources of new drugs and biopesticides. In addition, the identification and molecular characterization of Hymenoptera venom allergens have allowed for the rational design of component-resolved diagnosis of allergy, finally improving the outcome of venom immunotherapy (VIT). Until recently, a limited number of Hymenoptera venoms had been unveiled due to the technical limitations of the approaches used to date. Nevertheless, the application of novel techniques with high dynamic range has significantly increased the number of identified peptidic and proteinaceous toxins. Considering this, the present review summarizes the current knowledge about the most representative Hymenoptera venom peptides and proteins which are under study for a better understanding of the insect-caused envenoming process and the development of new drugs and biopesticides.

show abstract

Section: Kinin-related Peptidessupporting

confidence: 64%

Section: Kinin-related Peptidesmentioning

confidence: 97%

Section: Cytolytic Peptidesmentioning

confidence: 99%

Section: Neurotoxic Peptidesmentioning

confidence: 99%

See 2 more Smart Citations

Diversity of peptidic and proteinaceous toxins from social Hymenoptera venoms

Santos-Pinto

Pérez-Riverol

Lasa

et al. 2018

Toxicon

View full text Add to dashboard Cite

show abstract

“…Bradykinin-like peptide was found in wasp venoms as the first neurotoxic and pain-producing peptide [ 100 ]. It irreversibly blocks the synaptic transmission of nAChR in the insect central nervous system (CNS) [ 104 , 105 ]. While wasp kinins have remarkable sequence similarities to the main structure of mammalian bradykinin [-PPGF(T/S)P(F/L)-], most of them are longer than bradykinin or differ at position 3 or 6, where proline is replaced by hydroxyproline or serine is replaced by threonine (Thr 6 -bradykinin), which has a single extra hydroxyl or methyl group, respectively.…”

Section: Venom Peptidesmentioning

confidence: 99%

Differential Properties of Venom Peptides and Proteins in Solitary vs. Social Hunting Wasps

Lee

Baek

Yoon

2016

Toxins

View full text Add to dashboard Cite

The primary functions of venoms from solitary and social wasps are different. Whereas most solitary wasps sting their prey to paralyze and preserve it, without killing, as the provisions for their progeny, social wasps usually sting to defend their colonies from vertebrate predators. Such distinctive venom properties of solitary and social wasps suggest that the main venom components are likely to be different depending on the wasps’ sociality. The present paper reviews venom components and properties of the Aculeata hunting wasps, with a particular emphasis on the comparative aspects of venom compositions and properties between solitary and social wasps. Common components in both solitary and social wasp venoms include hyaluronidase, phospholipase A2, metalloendopeptidase, etc. Although it has been expected that more diverse bioactive components with the functions of prey inactivation and physiology manipulation are present in solitary wasps, available studies on venom compositions of solitary wasps are simply too scarce to generalize this notion. Nevertheless, some neurotoxic peptides (e.g., pompilidotoxin and dendrotoxin-like peptide) and proteins (e.g., insulin-like peptide binding protein) appear to be specific to solitary wasp venom. In contrast, several proteins, such as venom allergen 5 protein, venom acid phosphatase, and various phospholipases, appear to be relatively more specific to social wasp venom. Finally, putative functions of main venom components and their application are also discussed.

show abstract