Journal of Proteome Research · 2020 · 44 citations · 40 references
Life SciencesEntomologyMolecular BiologyInsect PhysiologyInsect SystematicsInsect ToxicologyInsecticide ToxicologyPeptide AnalysisVenom BiologyInsecticidal Activity AssaysNovel Insecticidal ProteinsProteomic IdentificationSnake Venom CompositionSnake Venom ProteomicsToxin BiochemistryVenom Composition AnalysisVenom Transcriptomics
Using an integrated transcriptomic and proteomic approach, we characterized the venom peptidome of the European red ant, Manica rubida. We identified 13 “myrmicitoxins” that share sequence similarities with previously identified ant venom peptides, one of them being identified as an EGF-like toxin likely resulting from a threonine residue modified by O-fucosylation. Furthermore, we conducted insecticidal assays of reversed-phase HPLC venom fractions on the blowfly Lucilia caesar, permitting us to identify six myrmicitoxins (i.e., U3-, U10-, U13-, U20-MYRTX-Mri1a, U10-MYRTX-Mri1b, and U10-MYRTX-Mri1c) with an insecticidal activity. Chemically synthesized U10-MYRTX-Mri1a, -Mri1b, -Mri1c, and U20-MYRTX-Mri1a irreversibly paralyzed blowflies at the highest doses tested (30–125 nmol·g–1). U13-MYRTX-Mri1a, the most potent neurotoxic peptide at 1 h, had reversible effects after 24 h (150 nmol·g–1). Finally, U3-MYRTX-Mri1a has no insecticidal activity, even at up to 55 nmol·g–1. Thus, M. rubida employs a paralytic venom rich in linear insecticidal peptides, which likely act by disrupting cell membranes.
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The Sequence Alignment/Map format and SAMtools
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Fast and accurate long-read alignment with Burrows–Wheeler transform
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