The insecticidal activity of recombinant nemertide toxin α-1 from Lineus longissimus towards pests and beneficial species

Bell, Jack P.; Sukiran, Nur Afiqah; Walsh, Stephen; Fitches, Elaine

doi:10.1016/j.toxicon.2021.04.003

Cited by 9 publications

(10 citation statements)

References 27 publications

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“…Furthermore, the toxin was shown to modulate insect Na V s at low nanomolar concentrations and mammalian Na V s in the μM range, suggesting a possible use for these peptides as bioinsecticides . This observation is supported by a recent study where pro-alpha-1 was expressed and tested against a selection of insects, demonstrating oral toxicity to aphids and brassica moths …”

supporting

confidence: 66%

“…19 This observation is supported by a recent study where pro-alpha-1 was expressed and tested against a selection of insects, demonstrating oral toxicity to aphids and brassica moths. 20 In the current work, we report the synthesis, oxidative folding, and functional characterization of native members of the α-nemertide family of peptide toxins. All peptides show activity on Artemia salina, and their activity on voltage-gated sodium channels of both invertebrate and vertebrate origin reveals selectivity as well as structure−activity relationships.…”

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confidence: 99%

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Functional Characterization of the Nemertide α Family of Peptide Toxins

et al. 2021

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Peptide toxins find use in medicine, biotechnology, and agriculture. They are exploited as pharmaceutical tools, particularly for the investigation of ion channels. Here, we report the synthesis and activity of a novel family of peptide toxins: the cystine-knotted α nemertides. Following the prototypic α-1 and -2 ( 1 and 2 ), six more nemertides were discovered by mining of available nemertean transcriptomes. Here, we describe their synthesis using solid phase peptide chemistry and their oxidative folding by using an improved protocol. Nemertides α-2 to α-7 ( 2 – 7 ) were produced to characterize their effect on voltage-gated sodium channels ( Blatella germanica BgNa V 1 and mammalian Na V s1.1–1.8). In addition, ion channel activities were matched to in vivo tests using an Artemia microwell assay. Although nemertides demonstrate high sequence similarity, they display variability in activity on the tested Na V s. The nemertides are all highly toxic to Artemia , with EC 50 values in the sub-low micromolar range, and all manifest preference for the insect BgNa V 1 channel. Structure–activity relationship analysis revealed key residues for Na V -subtype selectivity. Combined with low EC 50 values (e.g., Na V 1.1: 7.9 nM (α-6); Na V 1.3: 9.4 nM (α-5); Na V 1.4: 14.6 nM (α-4)) this underscores the potential utility of α-nemertides for rational optimization to improve selectivity.

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confidence: 66%

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confidence: 99%

Functional Characterization of the Nemertide α Family of Peptide Toxins

et al. 2021

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“…The rather rigid three-dimensional conformations imposed by their polycyclic architecture confer DRPs with a strong resistance towards in vivo enzymatic degradation. Taken together, these features contribute to establishing DRPs as an emerging lead compound for the development of novel peptide-based drugs and, more recently, as potential biopesticides in agronomical research [ 7 , 8 , 12 , 13 ]. For instance, a knottin DRP extracted from pea seeds, PA1b (Pea Albumin 1, subunit b, 37 amino acids (aa), three disulfide bonds) [ 9 , 12 , 14 ], is toxic to numerous insects, including aphids, cereal weevils, mosquitos and moths [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily

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Paquet

et al. 2022

IJMS

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Aphids (Hemiptera: Aphidoidea) are among the most detrimental insects for agricultural plants, and their management is a great challenge in agronomical research. A new class of proteins, called Bacteriocyte-specific Cysteine-Rich (BCR) peptides, provides an alternative to chemical insecticides for pest control. BCRs were initially identified in the pea aphid Acyrthosiphon pisum. They are small disulfide bond-rich proteins expressed exclusively in aphid bacteriocytes, the insect cells that host intracellular symbiotic bacteria. Here, we show that one of the A. pisum BCRs, BCR4, displays prominent insecticidal activity against the pea aphid, impairing insect survival and nymphal growth, providing evidence for its potential use as a new biopesticide. Our comparative genomics and phylogenetic analyses indicate that BCRs are restricted to the aphid lineage. The 3D structure of BCR4 reveals that this peptide belongs to an as-yet-unknown structural class of peptides and defines a new superfamily of defensins.

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“…Nemerteans have been studied for their ability to regenerate body parts ( Zattara et al ., 2019 ) and the potent venom neurotoxins secreted from the glandular epithelium of the proboscis ( Stricker & Cloney, 1983 ). The nemertide alpha-1 toxin from L. longissimus shows promise as an insecticide ( Bell et al ., 2021 ).…”

Section: Introductionmentioning

confidence: 99%