Oxotoxins, or oxytoxins, are a group of neurotoxins present in the venom of lynx spiders belonging to the genus Oxyopes, hence the name oxytoxin. They are disulfide-rich peptides. Only two types are so far reported from two different species, the larger oxytoxin 1 (OxyTx1) from Oxyopes kitabensis, and the smaller oxytoxin 2 (OxyTx2) from Oxyopes lineatus. OxyTx1, the first known oxytoxin, was discovered in 2002. It was found to enhance the lethal efficacy of the spider venom by acting together with oxyopinins.[1] It is composed of 69 amino acid residue, which are cross-linked by five disulfide bridges. It is a large peptide having a molecular mass of 8059.2 Da; but shows the size of 9,109.4 Da due to the presence of disulfide bridges. It is a potent insecticide, but non-toxic to mice up to 1 μg/20-g mouse. It acts synergistically with oxyopinins of the same venom to increase the insecticidal effect.
Both OxyTx1 and OxyTx2 were isolated in 2008 from O. lineatus.[2] Both of these toxins were found to block voltage-sensitive calcium ion channels. OxyTx2 is made up of 55 amino acid residues and has a molecular mass 6175.2 Da. It is less effective in causing paralysis in Spodoptera litura larvae than Oxytx1.
Types
editOxotoxins are classified as follows:
| Name | Recommended name | Size in Da | Amino acid residue | Toxicity (LD50) on S. litura |
|---|---|---|---|---|
| Oxytoxin 1 | Omega-oxotoxin-Ol1a | 8058.2 | 69 | 5.0 nmol/g |
| Oxytoxin 2 | Omega-oxotoxin-Ol1b | 6,186 | 55 | weak activity |
References
edit- ^ Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T (2002). "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. 277 (26): 23627–23637. doi:10.1074/jbc.M200511200. PMID 11976325.
- ^ Villegas E, Adachi-Akahane S, Bosmans F, Tytgat J, Nakajima T, Corzo G (2008). "Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels". Toxicon. 52 (2): 228–236. doi:10.1016/j.toxicon.2008.05.019. PMID 18606178.