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

Pinto, Ciro Pedro G.; Walker, Andrew A.; Robinson, Samuel D.; Chin, Yanni K.‐Y.; King, Glenn F.; Rossi, Gabriel Augusto Marques

doi:10.1016/j.toxicon.2021.09.002

Cited by 9 publications

(14 citation statements)

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“…The MS approach provided the identification of the HMWP. Protein identification indicated the PSP as an apolipophorin, previously detected in the venom apparatus of C. flavipes (Pinto et al, 2021;NCBI access: MZ442251). High molecular weight apolipophorins (>250 kDa) are classified as class I apolipophorins, or apolipophorins-I.…”

Section: Discussionmentioning

confidence: 89%

“…QBB01949.1), a species taxonomically | 355 close to C. flavipes. Moreover, a homology of 100% was observed among the peptide KSIKFSTDTELDKT and an apolipophorin from C. flavipes described in the proteotranscriptomic data of Pinto et al (2021). In addition to the apolipophorin, fatty acid synthase, glutamate synthase, and myosin heavy chain fragments also matched to C. chilonis and Cotesia congregata (Say), but with lower MS count per fragment (Table 2).…”

Section: R Esultsmentioning

confidence: 91%

“…Protein annotation with molecular weight >200 kDa was submitted to blastp tool with non-redundant NCBI (National Center for Biotechnology Information) proteins (nrNCBI). Main annotations were obtained for Cotesia species using MS and blastp data and searches on proteotranscriptome data from the C. flavipes venom apparatus (Pinto et al, 2021).…”

Section: Mass Spectrometry and Protein Identificationmentioning

confidence: 99%

“…In nature, there are still countless potential sources of molecules with distinct modes of action, most untapped or restricted to academic studies. For example, arachnid toxins (King & Hardy, 2013; Zhu et al, 2016; King, 2019), shell toxins (Gao et al, 2017), plant secondary compounds (Dang & van Damme, 2015), parasitoid‐derived proteins (Maiti et al, 2003; Rossi et al, 2012; Kim et al, 2016; Merlin et al, 2020; Pinto et al, 2021), as well microorganism‐derived toxins (Fan et al, 2007; Melo et al, 2016; Shen et al, 2017). Among those, parasitoid‐derived proteins may be considered the least exploited, even though being recognized as a rich source of bioactive molecules (Ali et al, 2015; Gao et al, 2016; Lin et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…By releasing several host regulation molecules, parasitoids alter host physiological functions, leading to successful development of the endoparasitoid larva. For example, parasitoids alter immune competence (Rana et al, 2002; Ali et al, 2015; Pinto et al, 2021), the endocrine system (Pennacchio et al, 1994), host nutrition and digestion (Cônsoli et al, 2001; Salvador & Cônsoli, 2008; Rossi et al, 2014), protein synthesis (Kadono‐Okuda et al, 1998), host metamorphosis (Shi et al, 2016), neuropeptide reprogramming (Shi et al, 2015), and enzymatic degradation of host fat body (Nakamatsu et al, 2002), among others (Rana et al, 2002; Caccia et al, 2012; Merlin & Cônsoli, 2019).…”

Section: Introductionmentioning

confidence: 99%

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First evidence of insecticidal potential of molecules produced during the parasitic phase of the endoparasitoid Cotesia flavipes

Santos

Silva

Balbuena

et al. 2022

Entomologia Exp Applicata

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Immature endoparasitoids develop inside their hosts. Consequently, endoparasitoids need to circumvent the action of the immune system and reprogram the physiology of their hosts to develop successfully. For this, parasitoids release host regulationrelated molecules into their host's hemolymph produced by the parasitoid itself or expressed in specific host cells infected by parasitoid symbiotic viruses. In addition to their roles in host regulation, these molecules may also present biotechnological potentials, such as for insecticidal purposes in crop protection. We performed a survey for the biotechnological potential of compounds present in the hemolymph serum with and without circulating cell contents of Diatraea saccharalis (Fabricius) (Lepidoptera: Crambidae) parasitized by Cotesia flavipes Cameron (Hymenoptera: Braconidae) as insecticides in feeding assays. Hemolymph serum from D. saccharalis larvae at 6 days after the start of the parasitism with and without circulating cell contents were collected and spread over artificial diet or over sugarcane leaves for feeding assays with D. saccharalis neonates. Hemolymph serum with or without circulating cell contents from non-parasitized D. saccharalis larvae at the same age were used as controls. Subsequently, hemolymph serum plus circulating cell contents was fractioned using molecular filters and fractions with different molecular weight range were used for feeding assays with D. saccharalis neonates. Feeding larvae with leaf disks amended with hemolymph serum plus circulating cell contents from parasitized hosts resulted in an increase of ca. 30% in the mortality of D. saccharalis neonates.After fractioning hemolymph serum plus circulating cell contents, feeding assays with the >100 or 3-10 kDa fractions did not result in the previously observed increase in larval mortality, but resulted in a reduction of leaf consumption by neonates. Finally, we selected a parasitism-specific protein band observed in the hemolymph >100 kDa fraction for mass spectrometry identification. This parasitism-specific protein was similar to hymenopteran apolipophorins-I. We conclude that there is an insecticidal potential in the hemolymph serum plus circulating cell contents of D. saccharalis larvae parasitized by C. flavipes and further investigations will be performed to identify, characterize, and uncover the biotechnological application of these molecules.

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Section: Discussionmentioning

confidence: 89%

Section: R Esultsmentioning

confidence: 91%

Section: Mass Spectrometry and Protein Identificationmentioning

confidence: 99%