Covalitoxin-II is a peptide toxin that is produced by the spider Coremiocnemis validus. It can induce excitatory, non-lethal behavioral symptoms like quivering and jerking in crickets.
Covalitoxin-II (Cvtx-II) is a toxin in the venom of Coremiocnemis validus (Singapore or Blue femur tarantula). [1] [2] This spider lives in South East Asian tropical forests. [1]
The toxin consists of 31 amino acids (ACSRAGENCYKSGRCCDGLYCKAYVVTCYKP). This sequence forms a peptide with a molecular weight of 3.4 kDa. It has six cysteine residues which form three disulphide bonds, between the specific amino acid locations 2&16, 19&21 and 15&28. [2] There is an equal distribution of hydrophilic, hydrophobic and neutral amino acids. Near the C-terminus there is a positively charged surface formed by conserved basic residues, which is thought to interact with an ion channel. [1] [3] The inhibitor cystine knot motif that is formed by the cysteine residues shows analogy to other spider toxins and can also be found in ω-conotoxins, which are present in the venom of cone snails. It has low homology with two peptides:
The specific target and mechanism of action of Cvtx-II are not yet clear. Based on its effect on behavior, it has been speculated that Cvtx-II targets sodium channel inactivation, analogous to some excitotoxins. [1]
Cvtx-II induces the following non-lethal symptoms in crickets:
Experiments have shown that these symptoms are not in present in cockroaches or mice after Cvtx-II injections. Therefore, Cvtx-II is thought to be an insect species-specific neurotoxic peptide. A dose of 0.2 µmol/g was necessary to immobilize or inactivate 50% of the insects (ID50). After 40–60 minutes, the immobilizing effects disappear. [1]
A conotoxin is one of a group of neurotoxic peptides isolated from the venom of the marine cone snail, genus Conus.
Poneratoxin is a paralyzing neurotoxic peptide made by the bullet ant Paraponera clavata. It prevents inactivation of voltage gated sodium channels and therefore blocks the synaptic transmission in the central nervous system. Specifically, poneratoxin acts on voltage gated sodium channels in skeletal muscle fibers, causing paralysis, and nociceptive fibers, causing pain. It is rated as a 4 plus on the Schmidt sting pain index, the highest possible rating with that system, and its effects can cause waves of pain up to twelve hours after a single sting. Schmidt describes it as "pure, intense, brilliant pain...like walking over flaming charcoal with a three-inch nail embedded in your heel." It is additionally being studied for its uses in biological insecticides.
Delta atracotoxin is a low-molecular-weight neurotoxic polypeptide found in the venom of the Sydney funnel-web spider.
Apamin is an 18 amino acid globular peptide neurotoxin found in apitoxin (bee venom). Dry bee venom consists of 2–3% of apamin. Apamin selectively blocks SK channels, a type of Ca2+-activated K+ channel expressed in the central nervous system. Toxicity is caused by only a few amino acids, in particular cysteine1, lysine4, arginine13, arginine14 and histidine18. These amino acids are involved in the binding of apamin to the Ca2+-activated K+ channel. Due to its specificity for SK channels, apamin is used as a drug in biomedical research to study the electrical properties of SK channels and their role in the afterhyperpolarizations occurring immediately following an action potential.
Spider toxins are a family of proteins produced by spiders which function as neurotoxins. The mechanism of many spider toxins is through blockage of calcium channels.
Birtoxin is a neurotoxin from the venom of the South African Spitting scorpion. By changing sodium channel activation, the toxin promotes spontaneous and repetitive firing much like pyrethroid insecticides do
Bestoxin is a neurotoxin from the venom of the South African spitting scorpion Parabuthus transvaalicus. Most likely, it targets sodium channel function, thus promoting spontaneous and repetitive neuronal firing. Following injection into mice, it causes non-lethal writhing behaviour.
AETX refers to a group of polypeptide neurotoxins isolated from the sea anemone Anemonia erythraea that target ion channels, altering their function. Four subtypes have been identified: AETX I, II, III and K, which vary in their structure and target.
BmKAEP is a neurotoxin from the venom of the Manchurian scorpion (Mesobuthus martensii). It is a β-toxin, which shift the activation voltage of sodium channels towards more negative potentials.
Raventoxins are neurotoxins from the venom of the spider Macrothele raveni.
Hainantoxins (HNTX) are neurotoxins from the venom of the Chinese bird spider Haplopelma hainanum. Hainantoxins specifically inhibit tetrodotoxin-sensitive Voltage-gated sodium channels, thereby causing blockage of neuromuscular transmission and paralysis. Currently, 13 different hainantoxins are known, but only HNTX-I, -II, -III, -IV and -V have been investigated in detail.
Huwentoxins (HWTX) are a group of neurotoxic peptides found in the venom of the Chinese bird spider Haplopelma schmidti. The species was formerly known as Haplopelma huwenum, Ornithoctonus huwena and Selenocosmia huwena. While structural similarity can be found among several of these toxins, HWTX as a group possess high functional diversity.
CSTX is a name given to a group of closely related neurotoxic peptides present in the venom of the wandering spider Cupiennius salei. There are twenty types so far described for this protein group. However, some are reclassified into cupiennins group of toxin, including CSTX-3, -4, -5, and -6, because of their chemical affinity. The first thirteen were isolated and identified in 1994 by Lucia Kuhn-Nentwig, Johann Schaller, and Wolfgang Nentwig of the Zoological Institute at the University of Bern, Switzerland. The different types are most likely the products of splicing variant of the same gene. They are all L-type calcium channel blockers, and also exhibit cytolytic activity by forming an alpha-helix across the cell membrane in mammalian neurons. They also inhibit voltage-gated calcium channels in insect neurons.
Oxyopinins are a group of peptide toxins present in the venom of lynx spiders belonging to the genus Oxyopes, from which they derive their name.
Hemitoxin (HTX; α-KTx6.15) is a 35-mer basic peptide from the venom of the Iranian scorpion Hemiscorpius lepturus, which reversibly blocks Kv1.1, Kv1.2 and Kv1.3voltage-gated K+ channels.
Halcurin is a polypeptide neurotoxin from the sea anemone Halcurias sp. Based on sequence homology to type 1 and type 2 sea anemone toxins it is thought to delay channel inactivation by binding to the extracellular site 3 on the voltage gated sodium channels in a membrane potential-dependent manner.
Agelenin, also called U1-agatoxin-Aop1a, is an antagonist of the presynaptic P-type calcium channel in insects. This neurotoxic peptide consists of 35 amino acids and can be isolated from the venom of the spider Allagelena opulenta.
ATX-II, also known as neurotoxin 2, Av2, Anemonia viridis toxin 2 or δ-AITX-Avd1c, is a neurotoxin derived from the venom of the sea anemone Anemonia sulcata. ATX-II slows down the inactivation of different voltage-gated sodium channels, including Nav1.1 and Nav1.2, thus prolonging action potentials.
μ-THTX-Cl6a, also known as Cl6a, is a 33-residue peptide toxin extracted from the venom of the spider Cyriopagopus longipes. The toxin acts as an inhibitor of the tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channel (NaV1.7), thereby causing sustained reduction of NaV1.7 currents.
GiTx1 (β/κ-theraphotoxin-Gi1a) is a peptide toxin present in the venom of Grammostola iheringi. It reduces both inward and outward currents by blocking voltage-gated sodium and potassium channels, respectively.