Characterization and biochemical analyses of venom from the ectoparasitic wasp Nasonia vitripennis (Walker) (hymenoptera: Pteromalidae)
Identifieur interne : 001341 ( Main/Exploration ); précédent : 001340; suivant : 001342Characterization and biochemical analyses of venom from the ectoparasitic wasp Nasonia vitripennis (Walker) (hymenoptera: Pteromalidae)
Auteurs : David B. Rivers [États-Unis] ; Fevzi Uckan [Turquie] ; Ekrem Ergin [Turquie]Source :
- Archives of Insect Biochemistry and Physiology [ 0739-4462 ] ; 2006-01.
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Abstract
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. Arch. Insect Biochem. Physiol. 61:24–41, 2006. © 2005 Wiley‐Liss, Inc.
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DOI: 10.1002/arch.20094
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Insect Biochem. 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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. Arch. Insect Biochem. Physiol. 61:24–41, 2006. © 2005 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>Turquie</li><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Rivers, David B" sort="Rivers, David B" uniqKey="Rivers D" first="David B." last="Rivers">David B. Rivers</name></region></country><country name="Turquie"><noRegion><name sortKey="Uckan, Fevzi" sort="Uckan, Fevzi" uniqKey="Uckan F" first="Fevzi" last="Uckan">Fevzi Uckan</name></noRegion><name sortKey="Ergin, Ekrem" sort="Ergin, Ekrem" uniqKey="Ergin E" first="Ekrem" last="Ergin">Ekrem Ergin</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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