Venom toxins

Gift, n. poison toxin venom, virus malice. 

The purpose of the venom is offensive while that of a poison is defensive, which in turn influences the characteristics of the toxin. Venoms, either large or small molecules, are usually variants of essential biological molecules such as lipids, steroids, histamines or other proteins. They are often mixtures with a specific mechanism of action such as paralyzing the nervous system. Poisons are designed to teach a predator that this is not a good meal. They usually cause more localized pain to discourage a predator, but depending on the dose and sensitivity of the individual, the poison can be deadly. 

The term embraces many aggression, defence or attack substances, released into the medium by various species, and of varied chemical composition poisons, toxins, venoms, antibiotics, antigerminatives, antimitotics, etc. They would appear to play a basic regulatory role in certain ecosystems, e.g. coral reefs (Burkholder, 1973). 

Thuesen, E.V., Kogure, K., Hashimoto, K., and Nemoto, T. 1988. Poison arrowworms A letrodo-toxin venom in the marine phylum Chaetonnatha. J. Exp. Mar. Biol. Ecol 116, 249-256. 

Protective and exploitive proteins Immunoglobulins Thrombin Eibrinogen Antifreeze proteins Snake and bee venom proteins Diphtheria toxin Rtcin... 

Recently, a variety of natural peptides that form transmembrane channels have been identified and characterized. Melittin (Figure 10.35) is a bee venom toxin peptide of 26 residues. The cecropins are peptides induced in Hyalophora cecropia (Figure 10.36) and other related silkworms when challenged by bacterial infections. These peptides are thought to form m-helical aggregates in mem-... 

Conotoxins are the venoms of the marine cone snails. The >500 Conus species produce >10,000 different toxins. All are cysteine-rich peptides of 10-30 amino... 

A second group of myotoxic toxins, found almost exclusively in the venoms of cobras, are the cytotoxins (often called cobratoxins, cytolysins, cardiotoxins, or direct lytic factors). These, rather than phospholipases, are almost certainly the primary cause of muscle damage following bites by cobras. Their mechanism of action is not properly known, but it is certainly the case that their action is potentiated by the presence of phospholipases in the venom, even if the phospholipases concerned are not, themselves, myotoxic. The cytotoxins of cobra venom possess no hydrolytic activity of any kind. 

A third group of myotoxic factors are very short polypeptides, devoid of hydrolytic activity. These toxins, found in the venom of a few species of North American rattlesnakes, cause a dilatation of sarcoplasmic reticulum and can cause severe muscle damage. 

Harris, J.B. (1990). Phospholipases in snake venoms and their effects on nerve and muscle. In Snake Toxins (Harvey, A.L., ed.), pp. 91-129, Pergamon Press, Oxford. 

Harris, J.B., Cullen, M.J. (1991). Muscle necrosis caused by snake venoms and toxins. Electron Microsc, Rev. 3, 183-211. 

Turning now to chemical attack, many predators immobilize their prey by injecting toxins, often neurotoxins, into them. Examples include venomous snakes, spiders, and scorpions. Some spider toxins (Quick and Usherwood 1990 Figure 1.3) are neurotoxic through antagonistic action upon glutamate receptors. The venom of some scorpions contains polypeptide neurotoxins that bind to the sodium channel. 

Immunologic abnormahties (eg, transfusion reactions, the presence in plasma of warm and cold antibodies that lyse red blood cells, and unusual sensitivity to complement) also fall in this class, as do toxins released by various infectious agents, such as certain bacteria (eg, Clostridium). Some snakes release venoms that act to lyse the red cell membrane (eg, via the action of phospholipases or proteinases). 

When a cone snail envenomates its prey, the latter is invariably paralyzed. In all cases, the paralytic toxins in the venom ("conotoxins") appear to be small peptides, most commonly with 3 disulfide bonds (although conotoxins with 2 or 4 S-S bonds... 

Between 6 and 10 homologous peptides have been extensively characterized for each toxin class. Although uj- and a-conotoxins have been isolated from several fish-hunting Conus species, x-conotoxins have so far been isolated only from C. geographus venom. 

The presence of toxins in C. geographus venom which block the response of vertebrate skeletal muscle to direct electrical stimulation was first detected by Endean et al. (14). A toxic component which reversibly blocked the generation of action... 

Like the other paralytic toxins from Conus venom, a-conotoxins are small and very tightly folded, structural features which may be advantageous for rapid paralysis of prey (1). a-Conotoxins are typically 13 to 15 amino acids long with two disulfide bridges (see Table III). In addition to the five a-conotoxins shown, two new a-conotoxins (SIA and SIB) from C. striatus have recently been isolated, sequenced, and chemically synthesized. SIA is very unusual because it is 19 amino acid residues long and it contains 6 cysteine residues, three of which are contiguous near the amino terminus (C. Ramilo et al., unpublished results). 

The a -, /z-, and a-conotoxins are the best characterized of the peptides isolated from Conus venoms so far. However, a large number of other peptides are found in these venoms. These comprise both paralytic toxins to immobilize the prey of the cone snail, and other biologically active peptides which are not themselves directly paralytic. Only the briefest overview of these peptide components will be presented here. 

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