Venom Information

Venom is the general term referring to any variety of toxins^[1] used by certain types of animals that inject it into their victims by the means of a bite or a sting.^[2] Unlike poison, which is ingested or inhaled into the victim's tract, administration of venom is usually directed into the lymphatic system itself for faster action.

Diversity

Invertebrates

Among animals using venom are spiders (see spider bite) and centipedes, which also inject venom through fangs; scorpions and stinging insects, which inject venom with a sting (which, in insects such as bees and wasps, is a modified egg-laying device – the ovipositor). Many caterpillars have defensive venom glands associated with specialized bristles on the body, known as urticating hairs, and can be lethal to humans (e.g., that of the Lonomia moth).

Because they are tasked to defend their hives and food stores, bees synthesize and employ an acidic venom (apitoxin) to cause pain in those that they sting, whereas wasps use a chemically different venom designed to paralyze prey, so it can be stored alive in the food chambers of their young. The use of venom is much more widespread than just these examples. Other insects, such as true bugs and many ants also produce venom. At least one ant species (Polyrhachis dives) has been shown to use venom topically for the sterilisation of pathogens^[3].

There are many other venomous invertebrates, including jellyfish and cone snails. The box jellyfish is the most venomous jellyfish in the world.

Fish

Venom can also be found in some fish, such as the cartilaginous fishes – stingrays, sharks, and chimaeras – and the teleost fishes including monognathus eels, catfishes, stonefishes and waspfishes, scorpionfishes and lionfishes, gurnards, rabbitfishes, surgeonfishes, scats, stargazers, weever, swarmfish.

Snakes and other reptiles

The reptiles most known to use venom are snakes, some species of which inject venom into their prey via fangs.

Snake venom is produced by glands below the eye (the mandibular gland) and delivered to the victim through tubular or channeled fangs. Snake venoms contain a variety of peptide toxins, including Proteases, which hydrolyze protein peptide bonds, nucleases, which hydrolyze the phosphodiester bonds of DNA, and neurotoxins, which disable signalling in the nervous system. Snakes use their venom principally for hunting, though they do not hesitate to employ it defensively. Venomous snake bites may cause a variety of symptoms, including pain, swelling, tissue necrosis, low blood pressure, convulsions, hemorrhage (varying by species of snake), respiratory paralysis, kidney failure, coma and death.

Prophylaxis

Doctors treat victims of a venomous bite with antivenom, which is created by dosing an animal such as a sheep, horse, goat, or rabbit with a small amount of the targeted venom. The immune system of the subject animal responds to the dose, producing antibodies to the venom's active molecules; the antibodies can then be harvested from the animal's blood and injected into bite victims to treat envenomation. This treatment can be used effectively only a limited number of times for a given individual, however, as a bite victim will ultimately develop antibodies to neutralize the foreign animal antigens injected into them as components of the antivenin. This is called sensitization. Even if a bite victim does not suffer a serious allergic reaction to the antivenom, his own, sensitized, immune system may destroy the antivenom before the antivenom can destroy the venom. Though most individuals never require even one treatment of antivenom in their lifetime, let alone several, those routinely exposed to snakes or other venomous animals may become sensitized to antivenom due to previous exposure.

Aristolochia rugosa and Aristolochia trilobata, or "Dutchman's Pipe", are recorded in a list of plants used worldwide and in the West Indies, South and Central America against snakebites and scorpion stings. Aristolochic acid inhibits inflammation induced by immune complexes, and nonimmunological agents (carrageenan or croton oil). Aristolochic acid inhibits the activity of snake venom phospholipase (PLA2) by forming a 1:1 complex with the enzyme. Since phospholipase enzymes play a significant part in the cascade leading to the inflammatory and pain response, their inhibition could lead to relief of problems from scorpion envenomation.

Other reptiles

Aside from snakes, venom is found in a few other reptiles such as the Mexican beaded lizard and Gila monster,and may be present in a few species of monitor lizards.

One such reptile that was previously thought of as being nonvenomous is the Komodo Dragon, Varanus komodoensis. It was then demonstrated through magnetic resonance imaging that the Komodo Dragon possess a mandibular gland with a major posterior compartment and 5 smaller anterior compartments.^[4] The scientists used mass spectrometry to show that the mixture of proteins present in the venom was as complex as the proteins found in snake venom.^[4][5]

Due to these recent studies investigating venom glands in squamates, lizards that were previously thought of as being nonvenomous are now being classified by some scientists as venomous because they possess a venom gland. This hypothetical clade, Toxicofera, includes all venomous squamates: the suborders Serpentes and Iguania and the families Varanidae, Anguidae, and Helodermatidae.^[6]

Mammals

Some mammals are also venomous, including solenodons, shrews, the slow loris, and the male platypus.

Amphibians

There are only a few species of venomous amphibians; certain salamandrid salamanders can extrude sharp venom-tipped ribs.^[7][8]

Dinosaurs

Sinornithosaurus, a genus of feathered dromaeosaurid dinosaur, may have had a venomous bite. This theory is still being disputed. The theropod Dilophosaurus is commonly depicted in popular culture as being venomous, but this portrayal is not considered likely by the scientific community.

See also

• Envenomation
• Schmidt Sting Pain Index
• Big Four (Indian snakes)
• List of venomous animals

References

1. ^ "venom" at Dorland's Medical Dictionary
2. ^ "venom - Definition from the Merriam-Webster Online Dictionary". http://www.merriam-webster.com/dictionary/venom. Retrieved 2008-12-13.
3. ^ Graystock, Peter; Hughes, William O. H. (2011). "Disease resistance in a weaver ant, Polyrhachis dives, and the role of antibiotic-producing glands". Behavioral Ecology and Sociobiology. doi:10.1007/s00265-011-1242-y.
4. ^ ^{a b} Bryan G. Fry, Stephen Wroec, Wouter Teeuwissed, et al., (University of Melbourne): PNAS, publisched online, doi:10.1073/pnas.0810883106, A central role for venom in predation by Varanus komodoensis (Komodo Dragon) and the extinct giant Varanus (Megalania) priscus'
5. ^ Fry, B. G., W. Wuster, S. F. R. Ramjan, T. Jackson, P. Martelli, and R. M. Kini. 2003c. Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: Evolutionary and toxinological implications. Rapid Communications in Mass Spectrometry 17:2047-2062.
6. ^ Fry, BG; Vidal, N; Norman, JA; Vonk, FJ; Scheib, H; Ramjan, SF; Kuruppu, S; Fung, K et al. (February 2006). "Early evolution of the venom system in lizards and snakes" (PDF). Nature 439 (7076): 584–588. doi:10.1038/nature04328. ISSN 0028-0836. PMID 16292255. http://www.nature.com/nature/journal/v439/n7076/abs/nature04328.html.
7. ^ http://www.askabiologist.org.uk/punbb/viewtopic.php?id=1494
8. ^ Nowak, R. T.; Brodie, E. D. (1978). "Rib Penetration and Associated Antipredator Adaptations in the Salamander Pleurodeles waltl (Salamandridae)". Copeia 1978 (3): 424–429. doi:10.2307/1443606.

Bibliography

• Smith WL, Wheeler WC (2006). "Venom evolution widespread in fishes: a phylogenetic road map for the bioprospecting of piscine venoms". J. Hered. 97 (3): 206–17. doi:10.1093/jhered/esj034. PMID 16740627. http://jhered.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=16740627.

• Lans C, Harper T, Georges K, Bridgewater E (2001). "Medicinal and ethnoveterinary remedies of hunters in Trinidad". BMC Complement Altern Med 1: 10. doi:10.1186/1472-6882-1-10. PMC 60997. PMID 11737880. http://www.biomedcentral.com/1472-6882/1/10.

• Fry, B. G., N. Vidal, J. A. Norman, F. J. Vonk, H. Scheib, S. F. R. Ramjan, S. Kuruppu, K. Fung, S. B. Hedges, M. K. Richardson, W. C. Hodgson, V. Ignjatovic, R. Summerhayes, and E. Kochva. 2006. Early evolution of the venom system in lizards and snakes. Nature (London) 439:584-588.

• Fry, B. G., S. Wroe, W. Teeuwisse, M. J. P. van Osch, K. Moreno, J. Ingle, C. McHenry, T. Ferrara, P. Clausen, H. Scheib, K. L. Winter, L. Greisman, K. Roelants, L. van der Weerd, C. J. Clemente, E. Giannakis, W. C. Hodgson, S. Luz, P. Martelli, K. Krishnasamy, E. Kochva, H. F. Kwok, D. Scanlon, J. Karas, D. M. Citron, E. J. C. Goldstein, J. E. Mcnaughtan, and J. A. Norman. 2009b. A central role for venom in predation by Varanus komodoensis (Komodo Dragon) and the extinct giant Varanus (Megalania) priscus. Proceedings of the National Academy of Sciences of the United States of America 106:8969-8974.

• Fry, B. G., W. Wuster, S. F. R. Ramjan, T. Jackson, P. Martelli, and R. M. Kini. 2003c. Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: Evolutionary and toxinological implications. Rapid Communications in Mass Spectrometry 17:2047-2062.

Categories:

• Toxins

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See Also:

• Venom