Identification of an aspartylglucosaminidase-like protein in the venom of the parasitic wasp Asobara tabida (Hymenoptera: Braconidae)

Moreau, Sébastien; Cherqui, Anas; Doury, Géraldine; Dubois, Frédéric; Fourdrain, Yvelise; Sabatier, Laurence; Bulet, Philippe; Saarela, Jani; Prévost, Geneviève; Giordanengo, Philippe

doi:10.1016/j.ibmb.2004.03.001

Cited by 35 publications

(38 citation statements)

References 39 publications

(41 reference statements)

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“…Accordingly, several labs have attempted to identify venom proteins from Drosophila parasitoid wasps using both single gene and high-throughput sequencing methods. [45][46][47][48][49][50][51] Most notable are recent attempts at understanding Drosophila parasitoid wasp virulence using approaches that combine highthroughput transcriptomics with venom proteomics. 18,50,51 These studies have identified a large number of venom proteins from 3 Drosophila parasitoid species (Ganaspis sp.1, L. boulardi, and L. heterotoma) and have revealed that these venoms contain unique putative virulence factors, in keeping with their distinct virulence mechanisms.…”

Section: Exploiting Parasitoid Virulence Activities To Study Host Immmentioning

confidence: 99%

Parasitoid wasp virulence

Mortimer

2013

Fly

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Section: Exploiting Parasitoid Virulence Activities To Study Host Immmentioning

confidence: 99%

Parasitoid wasp virulence

Mortimer

2013

Fly

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“…An aspartylglucosaminidase (AGA)-like protein was found in the venom of the endoparasitic wasp Asobara tabida, which had a polymeric conformation and was formed of 30 and 18 kD subunits. The enzyme usually had the analogous activity of lysosomal enzymes, stored in the reservoir of a parasitoid as a precursor molecule (Moreau et al, 2004). Baker et al (2005) identified a homologous series of five chemical classes from the mixture in the Dufour glands and venoms of Bracon cephi and B. lissogaster, and parasitoids of the wheat stem sawfly, Cephus cinctus.…”

Section: Classes Components and Properties Of Toxinsmentioning

confidence: 99%

Ecological mechanisms and prospects for utilization of toxins from parasitic hymenopterans

Wang

Yang

2008

Front. For. China

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Insects in the order Hymenoptera defend themselves, attack prey and regulate hosts using toxins that are effective in small quantities. In this study, advances in the researches on parasitic hymenopteran toxins are summarized in terms of the production, categories, components, properties, ecological functions and mechanisms. The glands that produce venoms derive from the ectoderm tissue and evolve from the accessory glands of the reproductive system. Venoms are excreted by the poison gland or acid gland of mature female wasps and stored in reservoirs. The components of insect toxins are very complicated, and hymenopteran venoms contain alkanes, alcohols, aldehydes, ketones, organic acids, esters, lactones, proteins, polypeptides, enzymes, amines and other compounds. Toxins of parasitic hymenoptera play an important adaptive role. They can increase the probability of successful oviposition by paralyzing hosts, enhancing offspring survival by inhibiting host development and immunoreaction, and improving the nutrition available for their progeny by disturbing the hosts' physiological response. Venoms of the ectoparasitoids often lead to arrested development, permanent paralysis and even death of hosts. These toxins are usually broad-spectrum and act on the central nervous system or at the neuro-muscular junction. While most endoparasitoids are koinobionts, these parasitoids can regulate the physiology and development of the hosts, but no longer paralyze the hosts permanently. Also, they kill the hosts in a concealed but safe position after the hosts cocoon or build their pupal cells. Venoms of koinobiont parasitoids can contain polydnaviruses (PDV) that regulate the growth and development of the hosts by inhibiting the immune system and influencing the metamorphosis of hosts. Thus, PDVs are commensal and mutualistic, but non-pathogenic, with parasitoids at the molecular level. Promising prospects for the utilization of insect toxins, especially as medicines or specific bioinsecticides, are discussed. Because insect toxins are mixtures of complex ingredients and are usually produced in small quantities, isolation and purification of all the ingredients with bioactivity are needed for biochemical and toxicological research and for practical application.

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“…The infrared spectrum also revealed the presence of phosphorus-containing structures, typical of enzymes, in the venom. Though the presence of enzymatic activity in N. vitripennis venom has yet to be confirmed, venoms from several endoparasitic species and social Hymenoptera have been shown to contain multiple types of enzymes (Moreau et al, 2004;Parkinson et al, 2001;2002a,b;Piek and Spanjier, 1986;Schmidt, 1982;Uçkan et al, 2004). Enzyme activity, however, does not likely account for the ability of venom from N. vitripennis to arrest host development or evoke death as crude venom preparations contained the protease inhibitor PMSF as well as the chelating agent EDTA, and high concentrations of anti-phenoloxidase antibodies had no influence on venom activity.…”

Section: January 2006mentioning

confidence: 99%

Characterization and biochemical analyses of venom from the ectoparasitic waspNasonia vitripennis (Walker) (hymenoptera: Pteromalidae)

Rivers

Uçkan

Ergın

2005

Arch. Insect Biochem. Physiol.

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During parasitism, the ectoparasitic wasp Nasonia vitripennis (Walker) (Hymenoptera: Pteromalidae) induces a developmental arrest in host pupae that is sustained until the fly is either consumed by developing larvae or the onset of death. Bioassays using fluids collected from the female reproductive system (calyx, alkaline gland, acid gland, and venom reservoir) indicated that the venom gland and venom reservoir are the sources of the arrestant and inducer(s) of death. Infrared spectroscopic analyses revealed that crude venom is acidic and composed of amines, peptides, and proteins, which apparently are not glycosylated. Reversed phase high performance liquid chromatography (HPLC) and sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the proteinaceous nature of venom and that it is composed mostly of mid to high molecular weight proteins in the range of 13 to 200.5 kilodaltons (kDa). Ammonium sulfate precipitation and centrifugal size exclusion membranes were used to isolate venom proteins. SDS-PAGE protein profiles of the isolated venom fractions displaying biological activity suggest that multiple proteins contribute to arresting host development and eliciting death. Additionally, HPLC fractionation coupled with use of several internal standards implied that two of the low molecular weight proteins were apamin and histamine. However, in vitro assays using BTI-TN-5B1-4 cells contradict the presence of these agents. Abbreviations used: HPLC = high performance liquid chromatography; I.R. = infrared spectroscopy; kDa = kilodalton; LC 99 = lethal concentration to kill 100% of population; LD = light-dark; MWCO = molecular weight cutoff; SDS-PAGE = sodium dodecyl sulfate polyacrylamide gel electrophoresis; TFA = trifluoroacetic acid; VRE = venom reservoir equivalent.

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Identification of an aspartylglucosaminidase-like protein in the venom of the parasitic wasp Asobara tabida (Hymenoptera: Braconidae)

Cited by 35 publications

References 39 publications

Parasitoid wasp virulence

Parasitoid wasp virulence

Ecological mechanisms and prospects for utilization of toxins from parasitic hymenopterans

Characterization and biochemical analyses of venom from the ectoparasitic waspNasonia vitripennis (Walker) (hymenoptera: Pteromalidae)

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