Abstract
Australian funnel-web spiders are relatively large primitive hunting spiders. Male Atrax robustus spiders have been responsible for a number of human deaths. Venom was collected from the species Hadronyche infensa (Hickman) [female], H. formidabilis [male and female], H. versuta [female], and A. robustus (Cambridge) [male] and was fractionated by high performance liquid chromatography. This resulted in the isolation and purification of a homologous series of 7 insecticidal peptides of relatively low molecular mass (approximately 4kDa). The amino acid sequences of these toxins consisted of 36 or 37 amino acids and were named atracotoxins. For the major bioassay of these toxins, we used the cotton bollworm, Helicoverpa armigera (Hubner), due to the great damage it causes to crops worldwide. These toxins, when injected subcutaneously into fifth or sixth instar larvae of Helicoverpa armigera,were lethal or caused an apparently irreversible writhing. The toxin from H. versuta venom showed no significant toxicity when subcutaneously injected into newborn mice. One of the toxins was found to have a free acid carboxyl terminus. These toxins have great potential as lead compounds for insecticide design or for incorporation in recombinant baculovirus insecticides.
Highlights
Venoms are increasingly being seen as a source of novel biological agents in fields as diverse as medicine and agriculture
Venom was collected from the species Hadronyche infensa (Hickman) [female], H. formidabilis [male and female], H. versuta [female], and A. robustus (Cambridge) [male] and was fractionated by high performance liquid chromatography
We have shown that venoms of Australian funnel-web spiders show insecticidal activity [2]
Summary
Venoms are increasingly being seen as a source of novel biological agents in fields as diverse as medicine and agriculture. Polyamine toxins cause fasteracting, reversible incapacitation of the target insect, whereas peptide toxins are associated with longer-term effects Other venoms such as those from scorpions and ants are rich sources of insect-active peptides [4, 16, 23, 24]. We report the biochemical examination of these venoms, revealing discrete active components which were purified and characterized as peptides toxic to insects. The existence of these toxins, which are relatively small and highly effective, encourages further research into field delivery systems either as lead structures for insecticide design or incorporated in recombinant baculovirus insecticides [9]. This work preceded and was the genesis of that of King et al [12]
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