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Review
. 2012 Mar;4(3):191-227.
doi: 10.3390/toxins4030191. Epub 2012 Mar 22.

Spider-venom peptides as bioinsecticides

Monique J Windley  1 , Volker Herzig, Sławomir A Dziemborowicz, Margaret C Hardy, Glenn F King, Graham M Nicholson
Affiliations
Review

Spider-venom peptides as bioinsecticides

Monique J Windley et al. Toxins (Basel). 2012 Mar.

Abstract

Over 10,000 arthropod species are currently considered to be pest organisms. They are estimated to contribute to the destruction of ~14% of the world's annual crop production and transmit many pathogens. Presently, arthropod pests of agricultural and health significance are controlled predominantly through the use of chemical insecticides. Unfortunately, the widespread use of these agrochemicals has resulted in genetic selection pressure that has led to the development of insecticide-resistant arthropods, as well as concerns over human health and the environment. Bioinsecticides represent a new generation of insecticides that utilise organisms or their derivatives (e.g., transgenic plants, recombinant baculoviruses, toxin-fusion proteins and peptidomimetics) and show promise as environmentally-friendly alternatives to conventional agrochemicals. Spider-venom peptides are now being investigated as potential sources of bioinsecticides. With an estimated 100,000 species, spiders are one of the most successful arthropod predators. Their venom has proven to be a rich source of hyperstable insecticidal mini-proteins that cause insect paralysis or lethality through the modulation of ion channels, receptors and enzymes. Many newly characterized insecticidal spider toxins target novel sites in insects. Here we review the structure and pharmacology of these toxins and discuss the potential of this vast peptide library for the discovery of novel bioinsecticides.

Keywords: bioinsecticides; cystine knot; insecticidal; peptide; pest control; spider venom.

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Figures

Figure 1
Figure 1
Distribution of spider-venom peptides. (A) Distribution of characterized araneomorph and mygalomorph spider-venom peptides organized by spider family. Abbreviated toxin family names are indicated on the right hand ordinate. Bars in dark grey indicate insecticidal toxins, while light grey bars are non-insecticidal peptides, including those with unknown activity, from the same spider family; (B) Mass distribution of characterized spider-venom peptides. Masses represent the monoisotopic oxidized mass sorted into 500 Da bins. The overlaid curve shows the cumulative total number of peptides. Dark grey columns show mass ranges dominated by proteins with sphingomyelinase D (SMase D) activity from Loxosceles spp., as well as latrotoxins (LTX), latroinsectoxins (LIT) and latrocrustatoxins (LCT) from Latrodectus spp. N-terminal fragments are not included in the data. Note the discontinuous abscissa in both panels. Data were collated from the ArachnoServer 2.0 Spider Toxin Database (www.arachnoserver.org; [70], accessed on 20 January 2012).
Figure 2
Figure 2
Precursor architecture and posttranslational modifications in spider-venom peptides. (A) All insecticidal spider-venom toxins display a classical prepropeptide paradigm except LITs (e.g., α-LIT-Lt1a) from Latrodectus spp. ω-AGTX-Aa1a from Agelenopsis aperta is a heterodimer consisting of a 66-residue major chain that is linked via a disulfide bond to a 3-residue minor chain; (B) Known PTMs in spider-venom peptides (dark grey bars) as well as probable PTMs (light grey bars) and those predicted from sequence homology (white bars); (C) Distribution of the number of disulfide bonds found in insecticidal spider toxins (dark grey bars) and non-insecticidal peptides (light grey bars). Peptides with unknown disulfide connectivity are not shown. Note the discontinuous axes in all panels. Data were collated from the ArachnoServer 2.0 Spider Toxin Database (www.arachnoserver.org; [70], accessed on 20 January 2012).
Figure 3
Figure 3
The ICK structural motif. Left-hand panels (A,B) show a schematic view of the 3D structures of typical representatives of the ICK structural motif: (A) The insecticidal peptide δ-AMATX-Pl1b (PDB 1V91) and (B) the insecticidal peptide ω-HXTX-Hv1a (formerly ω-ACTX-Hv1a; PDB 1AXH) showing the major pharmacophore residues. Panel (C) shows a schematic representation of the ICK motif depicting the formation of the cystine-knot and possible addition of the third β-strand. The dark arrow (β1) represents the additional β-strand not always present in ICK spider-venom peptides (i.e., present in A but not B). (D) Stereoview of the cystine-knot motif of κ-TRTX-Scg1a (formerly SGTx1). In all panels, β-strands are shown as gray arrows and disulfide bridges connecting cysteine residues are shown as dark gray lines with roman numerals.
Figure 4
Figure 4
Molecular targets of spider toxins. Dark grey bars represent invertebrate targets of insecticidal spider-venom toxins, while light grey bars represent vertebrate targets. Toxins may have more than one target and may be phylum-selective or non-selective. Abbreviations: SMase D, sphingomyelinase D; GluR, glutamate receptor; ASIC, acid-sensing ion channel; MSC, mechanosensitive channel; TRP, transient receptor potential; KCa, calcium-activated potassium channel. Note the discontinuous abscissa. Data were collated from the ArachnoServer 2.0 Spider Toxin Database (www.arachnoserver.org; [70], accessed on 19 January 2012).
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