| Literature DB >> 32182430 |
Axel Touchard1, Samira R Aili2, Nathan Téné1, Valentine Barassé1, Christophe Klopp3, Alain Dejean4,5, R Manjunatha Kini6,7, Laurent Coquet8, Thierry Jouenne8, Benjamin Lefranc9, Jérôme Leprince9, Pierre Escoubas10, Graham M Nicholson2, Michel Treilhou1, Elsa Bonnafé1.
Abstract
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.Entities:
Keywords: glycosylated toxin; peptidome; polycationic α-helix; predation; pyroglutamate; reversible neurotoxicity
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Year: 2020 PMID: 32182430 DOI: 10.1021/acs.jproteome.0c00048
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466