Spider-venom peptides: structure, pharmacology, and potential for control of insect pests.

  title={Spider-venom peptides: structure, pharmacology, and potential for control of insect pests.},
  author={Glenn F. King and Margaret C Hardy},
  journal={Annual review of entomology},
  • G. KingM. Hardy
  • Published 14 January 2013
  • Biology
  • Annual review of entomology
Spider venoms are an incredibly rich source of disulfide-rich insecticidal peptides that have been tuned over millions of years to target a wide range of receptors and ion channels in the insect nervous system. These peptides can act individually, or as part of larger toxin cabals, to rapidly immobilize envenomated prey owing to their debilitating effects on nervous system function. Most of these peptides contain a unique arrangement of disulfide bonds that provides them with extreme resistance… 

Versatile spider venom peptides and their medical and agricultural applications

  • N. J. SaezV. Herzig
  • Biology
    Toxicon : official journal of the International Society on Toxinology
  • 2019

Tying pest insects in knots: the deployment of spider-venom-derived knottins as bioinsecticides.

  • G. King
  • Biology, Chemistry
    Pest management science
  • 2019
It has been demonstrated that spider-knottin transgenes can be used to engineer faster-acting entomopathogens and insect-resistant crops.

Venoms of Heteropteran Insects: A Treasure Trove of Diverse Pharmacological Toolkits

The multiple ways venom is used by heteropterans suggests that further study will reveal heteropteran venom components with a wide range of bioactivities that may be recruited for use as bioinsecticides, human therapeutics, and pharmacological tools.

Diversity of peptide toxins from stinging ant venoms.

Isolation of an Orally Active Insecticidal Toxin from the Venom of an Australian Tarantula

It is shown that it is possible to isolate spider-venom peptides with high levels of oral insecticidal activity by directly screening for per os toxicity and the three-dimensional structure of OAIP-1 revealed that the three disulfide bonds form an inhibitor cystine knot motif; this structural motif provides the peptide with a high level of biological stability that probably contributes to its oral activity.

A short note on fusion proteins: An approach for insect-vector management

A large number of disulfide-rich (SS) insecticidal peptides have been isolated from spider venoms, which have desirable properties for development as bioinsecticides, including high potency, rapid speed of kill, lack of vertebrate toxicity, low production costs, and activity against a wide range of crop pests and disease vectors.

The biology and evolution of spider venoms.

The mechanisms that drive spider venom evolution are summarized and the need for genome-based studies to reconstruct the evolutionary history and physiological networks of spider venom compounds with more certainty is highlighted.

Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus

The insecticidal activity of U2‐SCTX‐Li1b, together with the large number of knottin peptides encoded in Loxosceles venom glands, suggests that studies of these venoms might facilitate future biotechnological applications of these toxins.



Spider-Venom Peptides as Bioinsecticides

The structure and pharmacology of many newly characterized insecticidal spider toxins target novel sites in insects and the potential of this vast peptide library for the discovery of novel bioinsecticides is discussed.

Pharmacology and biochemistry of spider venoms.

  • L. RashW. Hodgson
  • Biology, Chemistry
    Toxicon : official journal of the International Society on Toxinology
  • 2002

Spider-Venom Peptides as Therapeutics

The structure and pharmacology of spider-venom peptides that are being used as leads for the development of therapeutics against a wide range of pathophysiological conditions including cardiovascular disorders, chronic pain, inflammation, and erectile dysfunction are reviewed.


This review examines the function and three-dimensional structure of four families of novel insecticidal neurotoxins that have been isolated from the venom of Australian funnel-web spiders and suggests they should provide valuable tools for the pharmacological and structural characterization of insecticide targets.

Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom.

Eight linear cationic peptides with cytolytic and insecticidal activity, designated cyto-insectotoxins (CITs), were identified in Lachesana tarabaevi spider venom and are the first example of molecules showing equally potent antimicrobial and insecticide effects.

Venoms as a platform for human drugs: translating toxins into therapeutics

  • G. King
  • Biology, Chemistry
    Expert opinion on biological therapy
  • 2011
The current pipeline of venom-derived therapeutics is surveyed and the potential of peptide and protein drugs derived from venoms is critically examined, including an increasing industry focus on disulfide-rich venom peptides and the use of a broader array of molecular targets in order to develop venom-based therapeutics for treating a wider range of clinical conditions.

Antimicrobial and cytolytic peptides of venomous arthropods

This review provides an overview of antimicrobial peptides identified in the hemolymph of venomous arthropods, and especially of cytolytic peptides in their venom, and a dual role is proposed: acting as antimicrobials as well as increasing the potency of the venom by influencing excitable cells.

Orally active acaricidal peptide toxins from spider venom.

Australian funnel-web spiders: master insecticide chemists.