Venom composition of the endoparasitoid wasp Cotesia flavipes (Hymenoptera: Braconidae) and functional characterization of a major venom peptide

dc.contributor.authorPinto, Ciro P.G. [UNESP]
dc.contributor.authorWalker, Andrew A.
dc.contributor.authorRobinson, Samuel D.
dc.contributor.authorChin, Yanni K.-Y
dc.contributor.authorKing, Glenn F.
dc.contributor.authorRossi, Guilherme D. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionThe University of Queensland
dc.date.accessioned2022-04-28T19:44:45Z
dc.date.available2022-04-28T19:44:45Z
dc.date.issued2021-10-30
dc.description.abstractEndoparasitoid wasps use complex biochemical arsenals to suppress the normal humoral and cellular immune responses of their hosts in order to transform them into a suitable environment for development of their eggs and larvae. Venom injected during oviposition is a key component of this arsenal, but the functions of individual venom toxins are still poorly understood. Furthermore, there has been little investigation of the potential biotechnological use of these venom toxins, for example for control of agricultural pests. The endoparasitoid Cotesia flavipes (Hymenoptera: Braconidae) is a biocontrol agent reared in biofactories and released extensively in Brazil to control the sugarcane borer Diatraea saccharalis (Lepidoptera: Crambidae). The objectives of this work were to reveal venom components produced by C. flavipes and explore the function of a major venom peptide, Cf4. Using a combined proteomic/transcriptomic approach, we identified 38 putative venom toxins including both linear and disulfide-rich peptides, hydrolases, protease inhibitors, apolipophorins, lipid-binding proteins, and proteins of the odorant binding families. Because of its high abundance in the venom, we selected Cf4, a 33-residue peptide with three disulfide bonds, for synthesis and further characterization. We found that synthetic Cf4 reduced the capacity of D. saccharalis hemocytes to encapsulate foreign bodies without any effect on phenoloxidase activity, consistent with a role in disruption of the cellular host immune response. Feeding leaves coated with Cf4 to neonate D. saccharalis resulted in increased mortality and significantly reduced feeding compared to caterpillars fed untreated leaves, indicating that Cf4 is a potential candidate for insect pest control through ingestion. This study adds to our knowledge of endoparasitoid wasp venoms composition, host regulation mechanisms and their biotechnological potential for pest management.en
dc.description.affiliationSchool of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)
dc.description.affiliationInstitute for Molecular Bioscience The University of Queensland
dc.description.affiliationAustralian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Queensland
dc.description.affiliationUnespSchool of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)
dc.description.sponsorshipMedical Research Council
dc.description.sponsorshipAustralian Research Council
dc.description.sponsorshipIdAustralian Research Council: CE200100012
dc.format.extent1-12
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2021.09.002
dc.identifier.citationToxicon, v. 202, p. 1-12.
dc.identifier.doi10.1016/j.toxicon.2021.09.002
dc.identifier.issn1879-3150
dc.identifier.issn0041-0101
dc.identifier.scopus2-s2.0-85115177395
dc.identifier.urihttp://hdl.handle.net/11449/222446
dc.language.isoeng
dc.relation.ispartofToxicon
dc.sourceScopus
dc.subjectBiological control
dc.subjectDiatraea saccharalis
dc.subjectHost regulation
dc.subjectKoinobiont
dc.subjectPeptide toxin
dc.subjectToxin
dc.titleVenom composition of the endoparasitoid wasp Cotesia flavipes (Hymenoptera: Braconidae) and functional characterization of a major venom peptideen
dc.typeArtigo
unesp.author.orcid0000-0003-1296-6593 0000-0003-1296-6593[2]
unesp.author.orcid0000-0002-3518-0377[3]
unesp.author.orcid0000-0002-2308-2200 0000-0002-2308-2200[5]
unesp.author.orcid0000-0002-4249-5561[6]

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