Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae)

Skinner, Wayne S.; Dennis, Paula A.; Li, Jorge P.; Quistad, Gary B.

doi:10.1016/0041-0101(92)90049-b

Cited by 52 publications

(25 citation statements)

References 10 publications

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“…Among the arthropods, spiders are a rich source of peptide toxins targeting insects, and there is a growing interest in using these toxins for the development of bioinsecticides. The most potent of those toxins are active in the range of 10–100 pmol/g 2, 15,16 . In comparison, the active dose of α-1 at 1 µg/kg is equivalent to 300 fmol/g, highlighting the extraordinary potency of α-1.…”

Section: Discussionmentioning

confidence: 99%

Peptide ion channel toxins from the bootlace worm, the longest animal on Earth

Jacobsson

Andersson

Strand

et al. 2018

Sci Rep

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Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, named the α-nemertides, were discovered in the epidermal mucus of Lineus longissimus, the ‘bootlace worm’ known as the longest animal on earth. The most abundant peptide, the 31-residue long α-1, was isolated, synthesized, and its 3D NMR structure determined. Transcriptome analysis including 17 species revealed eight α-nemertides, mainly distributed in the genus Lineus. α-1 caused paralysis and death in green crabs (Carcinus maenas) at 1 µg/kg (~300 pmol/kg). It showed profound effect on invertebrate voltage-gated sodium channels (e.g. Blattella germanica Nav1) at low nanomolar concentrations. Strong selectivity for insect over human sodium channels indicates that α-nemertides can be promising candidates for development of bioinsecticidal agents.

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Section: Discussionmentioning

confidence: 99%

Peptide ion channel toxins from the bootlace worm, the longest animal on Earth

Jacobsson

Andersson

Strand

et al. 2018

Sci Rep

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“…In lepidopteran larvae, D. canities toxins caused a progressive spastic paralysis, with 50 % paralytic doses ranging from 0.38 to 3.18 nmol/g. Other insecticidal peptides were isolated from the venom of the trap-door spider, Aptostichus schlingeri [96]. Some of these toxins cause flaccid paralysis of insect larvae within 10 min of injection, and all were lethal within 24 h. The complete amino acid sequences (32 -76 residues) of six peptides were determined.…”

Section: Insecticidal Spptxs Without a Defined Mode Of Actionmentioning

confidence: 99%

Pharmacologically active spider peptide toxins

Corzo

Escoubas

2003

Cellular and Molecular Life Sciences (CMLS)

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Advances in mass spectrometry and peptide biochemistry coupled to modern methods in electrophysiology have permitted the isolation and identification of numerous novel peptide toxins from animal venoms in recent years. These advances have also opened up the field of spider venom research, previously unexplored due to methodological limitations. Many peptide toxins from spider venoms share structural features, amino acid composition and consensus sequences that allow them to interact with related classes of cellular receptors. They have become increasingly useful agents for the study of voltage-sensitive and ligand-gated ion channels and the discrimination of their cellular subtypes. Spider peptide toxins have also been recognized as useful agents for their antimicrobial properties and the study of pore formation in cell membranes. Spider peptide toxins with nanomolar affinities for their receptors are thus promising pharmacological tools for understanding the physiological role of ion channels and as leads for the development of novel therapeutic agents and strategies for ion channel-related diseases. Their high insecticidal potency can also make them useful probes for the discovery of novel insecticide targets in the insect nervous system or for the development of genetically engineered microbial pesticides.

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“…-Agatoxin-IVA, a neurotoxin isolated from the venom of the funnel web spider (Agelenopsis aperta), is a potent blocker of voltage-dependent P-type Ca 2ϩ channels in mammals (37). On the other hand, tachystatin C had 30 -33% sequence identity to insecticidal peptides isolated from spider venoms, such as -agatoxin II from A. aperta (38), aptotoxin VII from Aptostichus schlingeri (39), and curtatoxins II and III from Hololena curta (40) (Fig. 9B).…”

Section: Fig 6 Hemolytic Activity Of Tachystatin Cmentioning

confidence: 99%

Horseshoe Crab Hemocyte-derived Antimicrobial Polypeptides, Tachystatins, with Sequence Similarity to Spider Neurotoxins

Osaki¹,

Omotezako²,

Nagayama³

et al. 1999

Journal of Biological Chemistry

102

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Antimicrobial peptides, named tachystatins A, B, and C, were identified from hemocytes of the horseshoe crab Tachypleus tridentatus. Tachystatins exhibited a broad spectrum of antimicrobial activity against Gram-negative and Gram-positive bacteria and fungi. Of these tachystatins, tachystatin C was most effective. Tachystatin A is homologous to tachystatin B, but tachystatin C has no significant sequence similarity to tachystatins A and B. Tachystatins A and B showed sequence similarity to -agatoxin-IVA of funnel web spider venom, a potent blocker of voltage-dependent calcium channels. However, they exhibited no blocking activity of the P-type calcium channel in rat Purkinje cells. Tachystatin C also showed sequence similarity to several insecticidal neurotoxins of spider venoms. Tachystatins A, B, and C bound significantly to chitin. A causal relationship was observed between chitin binding activity and antifungal activity. Tachystatins caused morphological changes against a budding yeast, and tachystatin C had a strong cell lysis activity. The septum between mother cell and bud, a chitin-rich region, was stained by fluorescencelabeled tachystatin C, suggesting that the primary recognizing substance on the cell wall is chitin. As horseshoe crab is a close relative of the spider, tachystatins and spider neurotoxins may have evolved from a common ancestral peptide, with adaptive functions.

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Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae)

Cited by 52 publications

References 10 publications

Peptide ion channel toxins from the bootlace worm, the longest animal on Earth

Peptide ion channel toxins from the bootlace worm, the longest animal on Earth

Pharmacologically active spider peptide toxins

Horseshoe Crab Hemocyte-derived Antimicrobial Polypeptides, Tachystatins, with Sequence Similarity to Spider Neurotoxins

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