Structural Diversity and Basic/Acidic Residue Balance of Active Cysteine-Rich Insecticidal Peptides from Spiders
Among different cysteine-rich peptides produced by poisonous animals, the venom of spiders contains the most diverse cystine scaffolds with insecticidal activities but with a similar compact beta-sheet three-dimensional structure containing a significant amount of basic residues balanced with anionic ones, which could be substantial for both diffusion to the their cell target and binding to their protein receptors. The different cationic and anionic balance of the insecticidal spider peptides also suggests that other binding sites in the insect receptors could exist. Compared to the market and commercial pesticides, a minute selection of insect pests has been tested with the insecticidal spider toxins; however, they have shown strong activity against selected species of lepidopteran, dipteran, blattodean, and orthopteran with the inconvenience that the insecticidal peptides exert their lethal activity once injected into the hemolymph of insects. The knowledge on the precise targeting of insect receptors by robust ligands from spider venoms could be useful for understanding the molecular basis of toxin selectivity at the receptor level. This could also lead to the design of more effective and safer pesticides. This chapter addresses most of the insecticidal spider peptides already discovered with reported lethal or paralytic activity.
KeywordsInsecticidal Peptides Cysteine-rich Toxin Spider
This work was financed by grants from Dirección General de Asuntos del Personal Académico (DGAPA-UNAM), grant number IN204415, and SEP-CONACyT, grant number 240616.
- Coats JR. Insecticide mode of action. Academic; 2012.Google Scholar
- Corzo G, Villegas E, Gomez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. J Biol Chem. 2002;277:23627–37.CrossRefPubMedGoogle Scholar
- Down RE, Fitches EC, Wiles DP, Corti P, Bell HA, Gatehouse JA, Edwards JP. Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae). Pest Manag Sci. 2006;62:77–85.CrossRefPubMedGoogle Scholar
- Fitches E, Edwards MG, Mee C, Grishin E, Gatehouse AM, Edwards JP, Gatehouse JA. Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion. J Insect Physiol. 2004;50:61–71.CrossRefPubMedGoogle Scholar
- Schalle J, Kampfer U, Schurch S, Kuhn-Nentwig L, Haeberli S, Nentwig W. CSTX-9, a toxic peptide from the spider Cupiennius salei: amino acid sequence, disulphide bridge pattern and comparison with other spider toxins containing the cystine knot structure. Cell Mol Life Sci. 2001;58:1538–45.CrossRefPubMedGoogle Scholar
- Vassilevski AA, Fedorova IM, Maleeva EE, Korolkova YV, Efimova SS, Samsonova OV, Schagina LV, Feofanov AV, Magazanik LG, Grishin EV. Novel class of spider toxin: active principle from the yellow sac spider Cheiracanthium punctorium venom is a unique two-domain polypeptide. J Biol Chem. 2010;285:32293–302.PubMedCentralCrossRefPubMedGoogle Scholar