Journal
TOXICON
Volume 60, Issue 4, Pages 478-491Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2012.04.337
Keywords
Spider venom; Peptide; Inhibitor cystine knot; Voltage-gated sodium channel; Therapeutic; Analgesic; Insecticide; ArachnoServer; Na(v)1.7
Categories
Funding
- Australian Research Council [DP110103129, DP1095728]
- National Health & Medical Research Council [APP1034958]
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Voltage-gated sodium (Na-v) channels play a central role in the propagation of action potentials in excitable cells in both humans and insects. Many venomous animals have therefore evolved toxins that modulate the activity of Na-v channels in order to subdue their prey and deter predators. Spider venoms in particular are rich in Na-v channel modulators, with one-third of all known ion channel toxins from spider venoms acting on Na-v channels. Here we review the landscape of spider-venom peptides that have so far been described to target vertebrate or invertebrate Na-v channels. These peptides fall into 12 distinct families based on their primary structure and cysteine scaffold. Some of these peptides have become useful pharmacological tools, while others have potential as therapeutic leads because they target specific Na-v channel subtypes that are considered to be important analgesic targets. Spider venoms are conservatively predicted to contain more than 10 million bioactive peptides and so far only 0.01% of this diversity been characterised. Thus, it is likely that future research will reveal additional structural classes of spider-venom peptides that target Na-v channels. (c) 2012 Elsevier Ltd. All rights reserved.
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