Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na+ channels

• Published in: Toxicon (Oxford) Vol. 49; no. 4; pp. 550 - 560
• Main Authors: Bosmans, Frank, Tytgat, Jan
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 15.03.2007
• Subjects: Amino Acid Sequence; Animals; ATX-II; Cnidarian Venoms - chemistry; Cnidarian Venoms - pharmacology; Insecticide; Insecticides - chemistry; Insecticides - pharmacology; Ion Channel Gating; Molecular Sequence Data; Peptides - chemistry; Peptides - pharmacology; Pest Control, Biological; Sea anemone; Sea Anemones - physiology; Sequence Alignment; Site 3; Sodium Channel Blockers - pharmacology; Sodium Channels - drug effects; Species Specificity; Toxin; Voltage-gated sodium channel; Toxin; Site 3; Insecticide; ATX-II; Sea anemone; Voltage-gated sodium channel
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2006.11.029

Sea anemones produce a myriad of toxic peptides and proteins of which a large group acts on voltage-gated Na+ channels. However, in comparison to other organisms, their venoms and toxins are poorly studied. Most of the known voltage-gated Na+ channel toxins isolated from sea anemone venoms act on neurotoxin receptor site 3 and inhibit the inactivation of these channels. Furthermore, it seems that most of these toxins have a distinct preference for crustaceans. Given the close evolutionary relationship between crustaceans and insects, it is not surprising that sea anemone toxins also profoundly affect insect voltage-gated Na+ channels, which constitutes the scope of this review. For this reason, these peptides can be considered as insecticidal lead compounds in the development of insecticides.