Venom

Last updated

Wasp stinger with a droplet of venom Waspstinger1658-2.jpg
Wasp stinger with a droplet of venom

Venom or zootoxin is a type of toxin produced by an animal that is actively delivered through a wound by means of a bite, sting, or similar action. [1] [2] [3] The toxin is delivered through a specially evolved venom apparatus, such as fangs or a stinger, in a process called envenomation. [2] Venom is often distinguished from poison, which is a toxin that is passively delivered by being ingested, inhaled, or absorbed through the skin, [4] and toxungen, which is actively transferred to the external surface of another animal via a physical delivery mechanism. [5]

Contents

Venom has evolved in terrestrial and marine environments and in a wide variety of animals: both predators and prey, and both vertebrates and invertebrates. Venoms kill through the action of at least four major classes of toxin, namely necrotoxins and cytotoxins, which kill cells; neurotoxins, which affect nervous systems; myotoxins, which damage muscles; and haemotoxins, which disrupt blood clotting. Venomous animals cause tens of thousands of human deaths per year.

Venoms are often complex mixtures of toxins of differing types. Toxins from venom are used to treat a wide range of medical conditions including thrombosis, arthritis, and some cancers. Studies in venomics are investigating the potential use of venom toxins for many other conditions.

Evolution

The use of venom across a wide variety of taxa is an example of convergent evolution. It is difficult to conclude exactly how this trait came to be so intensely widespread and diversified. The multigene families that encode the toxins of venomous animals are actively selected, creating more diverse toxins with specific functions. Venoms adapt to their environment and victims, evolving to become maximally efficient on a predator's particular prey (particularly the precise ion channels within the prey). Consequently, venoms become specialized to an animal's standard diet. [6]

Mechanisms

Phospholipase A2, an enzyme in bee venom, releases fatty acids, affecting calcium signalling. 1poc.png
Phospholipase A2, an enzyme in bee venom, releases fatty acids, affecting calcium signalling.

Venoms cause their biological effects via the many toxins that they contain; some venoms are complex mixtures of toxins of differing types. Major classes of toxin in venoms include: [7]

Taxonomic range

Venom is widely distributed taxonomically, being found in both invertebrates and vertebrates, in aquatic and terrestrial animals, and among both predators and prey. The major groups of venomous animals are described below.

Arthropods

Venomous arthropods include spiders, which use fangs on their chelicerae to inject venom, and centipedes, which use forcipules  — modified legs — to deliver venom, while scorpions and stinging insects inject venom with a sting. In bees and wasps, the stinger is a modified ovipositor (egg-laying device). In Polistes fuscatus , the female continuously releases a venom that contains a sex pheromone that induces copulatory behavior in males. [16] In wasps such as Polistes exclamans , venom is used as an alarm pheromone, coordinating a response from the nest and attracting nearby wasps to attack the predator. [17] In some species, such as Parischnogaster striatula , venom is applied all over the body as an antimicrobial protection. [18]

Many caterpillars have defensive venom glands associated with specialized bristles on the body called urticating hairs. These are usually merely irritating, but those of the Lonomia moth can be fatal to humans. [19]

Bees synthesize and employ an acidic venom (apitoxin) to defend their hives and food stores, whereas wasps use a chemically different venom to paralyse prey, so their prey remains alive to provision the food chambers of their young. The use of venom is much more widespread than just these examples; many other insects, such as true bugs and many ants, also produce venom. [20] The ant species Polyrhachis dives uses venom topically for the sterilisation of pathogens. [21]

Other invertebrates

The fingernail-sized box jellyfish Malo kingi has among the most dangerous venom of any animal, causing Irukandji syndrome -- severe pain, vomiting, and rapid rise in blood pressure Irukandji-jellyfish-queensland-australia.jpg
The fingernail-sized box jellyfish Malo kingi has among the most dangerous venom of any animal, causing Irukandji syndrome⁠ — severe pain, vomiting, and rapid rise in blood pressure

There are venomous invertebrates in several phyla, including jellyfish such as the dangerous box jellyfish, [22] the Portuguese man-of-war (a siphonophore) and sea anemones among the Cnidaria, [23] sea urchins among the Echinodermata, [24] and cone snails [25] and cephalopods, including octopuses, among the Molluscs. [26]

Vertebrates

Fish

Venom is found in some 200 cartilaginous fishes, including stingrays, sharks, and chimaeras; the catfishes (about 1000 venomous species); and 11 clades of spiny-rayed fishes (Acanthomorpha), containing the scorpionfishes (over 300 species), stonefishes (over 80 species), gurnard perches, blennies, rabbitfishes, surgeonfishes, some velvetfishes, some toadfishes, coral crouchers, red velvetfishes, scats, rockfishes, deepwater scorpionfishes, waspfishes, weevers, and stargazers. [27]

Amphibians

Some salamanders can extrude sharp venom-tipped ribs. [28] [29] Two frog species in Brazil have tiny spines around the crown of their skulls which, on impact, deliver venom into their targets. [30]

Reptiles

PrairieRattlesnake.jpg
PDB 1rm8 EBI.jpg
The venom of the prairie rattlesnake, Crotalus viridis (left), includes metalloproteinases (example on the right) which help digest prey before eating.

Some 450 species of snake are venomous. [27] Snake venom is produced by glands below the eye (the mandibular glands) and delivered to the target 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 disrupt signalling in the nervous system. [31] Snake venom causes symptoms including pain, swelling, tissue necrosis, low blood pressure, convulsions, haemorrhage (varying by species of snake), respiratory paralysis, kidney failure, coma, and death. [32] Snake venom may have originated with duplication of genes that had been expressed in the salivary glands of ancestors. [33] [34]

Venom is found in a few other reptiles such as the Mexican beaded lizard, [35] the gila monster, [36] and some monitor lizards, including the Komodo dragon. [37] Mass spectrometry showed that the mixture of proteins present in their venom is as complex as the mixture of proteins found in snake venom. [37] [38] Some lizards possess a venom gland; they form a hypothetical clade, Toxicofera, containing the suborders Serpentes and Iguania and the families Varanidae, Anguidae, and Helodermatidae. [39]

Mammals

Euchambersia , an extinct genus of therocephalians, is hypothesized to have had venom glands attached to its canine teeth. [40]

A few species of living mammals are venomous, including solenodons, shrews, vampire bats, male platypuses, and slow lorises. [27] [41] Shrews have venomous saliva and most likely evolved their trait similarly to snakes. [42] The presence of tarsal spurs akin to those of the platypus in many non-therian Mammaliaformes groups suggests that venom was an ancestral characteristic among mammals. [43]

Extensive research on platypuses shows that their toxin was initially formed from gene duplication, but data provides evidence that the further evolution of platypus venom does not rely as much on gene duplication as was once thought. [44] Modified sweat glands are what evolved into platypus venom glands. Although it is proven that reptile and platypus venom have independently evolved, it is thought that there are certain protein structures that are favored to evolve into toxic molecules. This provides more evidence of why venom has become a homoplastic trait and why very different animals have convergently evolved. [13]

Venom and humans

Envenomation resulted in 57,000 human deaths in 2013, down from 76,000 deaths in 1990. [45] Venoms, found in over 173,000 species, have potential to treat a wide range of diseases, explored in over 5,000 scientific papers. [36]

In medicine, snake venom proteins are used to treat conditions including thrombosis, arthritis, and some cancers. [46] [47] Gila monster venom contains exenatide, used to treat type 2 diabetes. [36] Solenopsins extracted from fire ant venom has demonstrated biomedical applications, ranging from cancer treatment to psoriasis. [48] [49] A branch of science, venomics, has been established to study the proteins associated with venom and how individual components of venom can be used for pharmaceutical means. [50]

Resistance

CA Ground Squirrel on rock.jpg
Crotalus oreganus.jpg
The California ground squirrel is resistant to the Northern Pacific rattlesnake's powerful venom.

Venom is used as a trophic weapon by many predator species. The coevolution between predators and prey is the driving force of venom resistance, which has evolved multiple times throughout the animal kingdom. [51] The coevolution between venomous predators and venom-resistant prey has been described as a chemical arms race. [52] Predator/prey pairs are expected to coevolve over long periods of time. [53] As the predator capitalizes on susceptible individuals, the surviving individuals are limited to those able to evade predation. [54] Resistance typically increases over time as the predator becomes increasingly unable to subdue resistant prey. [55] The cost of developing venom resistance is high for both predator and prey. [56] The payoff for the cost of physiological resistance is an increased chance of survival for prey, but it allows predators to expand into underutilised trophic niches. [57]

The California ground squirrel has varying degrees of resistance to the venom of the Northern Pacific rattlesnake. [58] The resistance involves toxin scavenging and depends on the population. Where rattlesnake populations are denser, squirrel resistance is higher. [59] Rattlesnakes have responded locally by increasing the effectiveness of their venom. [60]

The kingsnakes of the Americas are constrictors that prey on many venomous snakes. [61] They have evolved resistance which does not vary with age or exposure. [55] They are immune to the venom of snakes in their immediate environment, like copperheads, cottonmouths, and North American rattlesnakes, but not to the venom of, for example, king cobras or black mambas. [62]

Ocellaris clownfish always live among venomous sea anemone tentacles and are resistant to the venom. Ocellaris clownfish, Flickr.jpg
Ocellaris clownfish always live among venomous sea anemone tentacles and are resistant to the venom.

Among marine animals, eels are resistant to sea snake venoms, which contain complex mixtures of neurotoxins, myotoxins, and nephrotoxins, varying according to species. [63] [64] Eels are especially resistant to the venom of sea snakes that specialise in feeding on them, implying coevolution; non-prey fishes have little resistance to sea snake venom. [65]

Clownfish always live among the tentacles of venomous sea anemones (an obligatory symbiosis for the fish), [66] and are resistant to their venom. [67] [68] Only 10 known species of anemones are hosts to clownfish and only certain pairs of anemones and clownfish are compatible. [69] [70] All sea anemones produce venoms delivered through discharging nematocysts and mucous secretions. The toxins are composed of peptides and proteins. They are used to acquire prey and to deter predators by causing pain, loss of muscular coordination, and tissue damage. Clownfish have a protective mucus that acts as a chemical camouflage or macromolecular mimicry preventing "not self" recognition by the sea anemone and nematocyst discharge. [71] [72] [73] Clownfish may acclimate their mucus to resemble that of a specific species of sea anemone. [73]

See also

Related Research Articles

<span class="mw-page-title-main">Cnidocyte</span> Explosive cell containing one giant secretory organelle (cnida)

A cnidocyte is an explosive cell containing one large secretory organelle called a cnidocyst that can deliver a sting to other organisms. The presence of this cell defines the phylum Cnidaria. Cnidae are used to capture prey and as a defense against predators. A cnidocyte fires a structure that contains a toxin within the cnidocyst; this is responsible for the stings delivered by a cnidarian. Cnidocytes are single-use cells that need to be continuously replaced.

<span class="mw-page-title-main">Rattlesnake</span> Group of venomous snakes of the genera Crotalus and Sistrurus

Rattlesnakes are venomous snakes that form the genera Crotalus and Sistrurus of the subfamily Crotalinae. All rattlesnakes are vipers. Rattlesnakes are predators that live in a wide array of habitats, hunting small animals such as birds and rodents.

<span class="mw-page-title-main">Snakebite</span> Injury caused by bite from snakes

A snakebite is an injury caused by the bite of a snake, especially a venomous snake. A common sign of a bite from a venomous snake is the presence of two puncture wounds from the animal's fangs. Sometimes venom injection from the bite may occur. This may result in redness, swelling, and severe pain at the area, which may take up to an hour to appear. Vomiting, blurred vision, tingling of the limbs, and sweating may result. Most bites are on the hands, arms, or legs. Fear following a bite is common with symptoms of a racing heart and feeling faint. The venom may cause bleeding, kidney failure, a severe allergic reaction, tissue death around the bite, or breathing problems. Bites may result in the loss of a limb or other chronic problems or even death.

<span class="mw-page-title-main">Snake venom</span> Highly modified saliva containing zootoxins

Snake venom is a highly toxic saliva containing zootoxins that facilitates in the immobilization and digestion of prey. This also provides defense against threats. Snake venom is injected by unique fangs during a bite, whereas some species are also able to spit venom.

<span class="mw-page-title-main">Venomous mammal</span> Venom-producing animals of the class Mammalia

Venomous mammals are animals of the class Mammalia that produce venom, which they use to kill or disable prey, to defend themselves from predators or conspecifics or in agonistic encounters. Mammalian venoms form a heterogeneous group with different compositions and modes of action, from four orders of mammals: Eulipotyphla, Monotremata, Primates, and Chiroptera. To explain the rarity of venom delivery in Mammalia, Mark Dufton of the University of Strathclyde has suggested that modern mammalian predators do not need venom because they are able to kill quickly with their teeth or claws, whereas venom, no matter how sophisticated, requires time to disable prey.

<i>Crotalus scutulatus</i> Species of snake

Crotalus scutulatus is known commonly as the Mohave Rattlesnake. Other common English names include Mojave Rattlesnake and, referring specifically to the nominate (northern) subspecies: Northern Mohave Rattlesnake and Mojave Green Rattlesnake, the latter name undoubtedly acquiescing to the widely used colloquial name “Mojave green”. Campbell and Lamar (2004) supported the English name “Mohave (Mojave) rattlesnake” with some reluctance because so little of the snake’s range lies within the Mojave Desert.

<span class="mw-page-title-main">Chinese red-headed centipede</span> Subspecies of centipede

The Chinese red-headed centipede, also known as the Chinese red head, is a centipede from East Asia. It averages 20 cm (8 in) in length and lives in damp environments.

<span class="mw-page-title-main">Venomous snake</span> Species of the suborder Serpentes that produce venom

Venomous snakes are species of the suborder Serpentes that are capable of producing venom, which they use for killing prey, for defense, and to assist with digestion of their prey. The venom is typically delivered by injection using hollow or grooved fangs, although some venomous snakes lack well-developed fangs. Common venomous snakes include the families Elapidae, Viperidae, Atractaspididae, and some of the Colubridae. The toxicity of venom is mainly indicated by murine LD50, while multiple factors are considered to judge the potential danger to humans. Other important factors for risk assessment include the likelihood that a snake will bite, the quantity of venom delivered with the bite, the efficiency of the delivery mechanism, and the location of a bite on the body of the victim. Snake venom may have both neurotoxic and hemotoxic properties. There are about 600 venomous snake species in the world.

<span class="mw-page-title-main">Myotoxin</span>

Myotoxins are small, basic peptides found in snake venoms and lizard venoms. This involves a non-enzymatic mechanism that leads to severe muscle necrosis. These peptides act very quickly, causing instantaneous paralysis to prevent prey from escaping and eventually death due to diaphragmatic paralysis.

<span class="mw-page-title-main">Venomous fish</span> Fish that have the ability to produce toxins

Venomous fish are species of fish which produce strong mixtures of toxins harmful to humans which they deliberately deliver by means of a bite, sting, or stab, resulting in an envenomation. As a contrast, poisonous fish also produce a strong toxin, but they do not bite, sting, or stab to deliver the toxin, instead being poisonous to eat because the human digestive system does not destroy the toxin they contain in their bodies. Venomous fish do not necessarily cause poisoning if they are eaten, as the digestive system often destroys the venom.

<span class="mw-page-title-main">Platypus venom</span> Venom produced by the platypus

The platypus is one of the few living mammals to produce venom. The venom is made in venom glands that are connected to hollow spurs on their hind legs; it is primarily made during the mating season. While the venom's effects are described as extremely painful, it is not lethal to humans. Many archaic mammal groups possess similar tarsal spurs, so it is thought that, rather than having developed this characteristic uniquely, the platypus simply inherited this characteristic from its antecedents. Rather than being a unique outlier, the platypus is the last demonstration of what was once a common mammalian characteristic, and it can be used as a model for non-therian mammals and their venom delivery and properties.

Taipoxin is a potent myo- and neurotoxin that was isolated from the venom of the coastal taipan Oxyuranus scutellatus or also known as the common taipan. Taipoxin like many other pre-synaptic neurotoxins are phospholipase A2 (PLA2) toxins, which inhibit/complete block the release of the motor transmitter acetylcholine and lead to death by paralysis of the respiratory muscles (asphyxia). It is the most lethal neurotoxin isolated from any snake venom to date.

<span class="mw-page-title-main">Sierra newt</span> Species of amphibian

The Sierra newt is a newt found west of the Sierra Nevada, from Shasta county to Tulare County, in California, Western North America.

<span class="mw-page-title-main">Crotamine</span>

Crotamine is a toxin present in the venom of the South American rattlesnake. It is a 42-residue long protein containing 11 basic residues and 6 cysteines. It has also been isolated from the venom of North American prairie rattlesnake, Crotalus viridis viridis. It was first isolated and purified by Brazilian scientist José Moura Gonçalves, and later intensively studied by his group of collaborators at the Medical School of Ribeirão Preto of the University of São Paulo.

<span class="mw-page-title-main">Caudal luring</span> Form of aggressive mimicry where the predator attracts prey using its tail

Caudal luring is a form of aggressive mimicry characterized by the waving or wriggling of the predator's tail to attract prey. This movement attracts small animals who mistake the tail for a small worm or other small animal. When the animal approaches to prey on the worm-like tail, the predator will strike. This behavior has been recorded in snakes, sharks, and eels.

α-Neurotoxin Group of neurotoxic peptides found in the venom of snakes

α-Neurotoxins are a group of neurotoxic peptides found in the venom of snakes in the families Elapidae and Hydrophiidae. They can cause paralysis, respiratory failure, and death. Members of the three-finger toxin protein family, they are antagonists of post-synaptic nicotinic acetylcholine receptors (nAChRs) in the neuromuscular synapse that bind competitively and irreversibly, preventing synaptic acetylcholine (ACh) from opening the ion channel. Over 100 α-neurotoxins have been identified and sequenced.

Venom optimization hypothesis, also known as venom metering, is a biological hypothesis which postulates that venomous animals have physiological control over their production and use of venoms. It explains the economic use of venom because venom is a metabolically expensive product, and that there is a biological mechanism for controlling their specific use. The hypothetical concept was proposed by Esther Wigger, Lucia Kuhn-Nentwig, and Wolfgang Nentwig of the Zoological Institute at the University of Bern, Switzerland, in 2002.

<span class="mw-page-title-main">Evolution of snake venom</span> Origin and diversification of snake venom through geologic time

Venom in snakes and some lizards is a form of saliva that has been modified into venom over its evolutionary history. In snakes, venom has evolved to kill or subdue prey, as well as to perform other diet-related functions. While snakes occasionally use their venom in self defense, this is not believed to have had a strong effect on venom evolution. The evolution of venom is thought to be responsible for the enormous expansion of snakes across the globe.

Venomics is the large-scale study of proteins associated with venom. Venom is a toxic substance secreted by animals, which is typically injected either offensively or defensively into prey or aggressors, respectively.

References

  1. ↑ "venom" "at Dorland's Medical Dictionary
  2. 1 2 Gupta, Ramesh C. (24 March 2017). Reproductive and developmental toxicology. Saint Louis. pp. 963–972. ISBN   978-0-12-804240-3. OCLC   980850276.{{cite book}}: CS1 maint: location missing publisher (link)
  3. ↑ Chippaux, JP; Goyffon, M (2006). "[Venomous and poisonous animals--I. Overview]". Médecine Tropicale (in French). 66 (3): 215–20. ISSN   0025-682X. PMID   16924809.
  4. ↑ "Poison vs. Venom". Australian Academy of Science . 3 November 2017. Retrieved 17 April 2022.
  5. ↑ Nelsen, D. R., Nisani, Z., Cooper, A. M., Fox, G. A., Gren, E. C., Corbit, A. G., & Hayes, W. K. (2014). "Poisons, toxungens, and venoms: redefining and classifying toxic biological secretions and the organisms that employ them". Biological Reviews, 89(2), 450-465. doi:10.1111/brv.12062. PMID: 24102715.
  6. ↑ Kordiš, D.; Gubenšek, F. (2000). "Adaptive evolution of animal toxin multigene families". Gene. 261 (1): 43–52. doi:10.1016/s0378-1119(00)00490-x. PMID   11164036.
  7. ↑ Harris, J. B. (September 2004). "Animal poisons and the nervous system: what the neurologist needs to know". Journal of Neurology, Neurosurgery & Psychiatry. 75 (suppl_3): iii40–iii46. doi:10.1136/jnnp.2004.045724. PMC   1765666 . PMID   15316044.
  8. ↑ Raffray, M.; Cohen, G. M. (1997). "Apoptosis and necrosis in toxicology: a continuum or distinct modes of cell death?". Pharmacology & Therapeutics. 75 (3): 153–177. doi:10.1016/s0163-7258(97)00037-5. PMID   9504137.
  9. ↑ Dutertre, Sébastien; Lewis, Richard J. (2006). "Toxin insights into nicotinic acetylcholine receptors". Biochemical Pharmacology. 72 (6): 661–670. doi:10.1016/j.bcp.2006.03.027. PMID   16716265.
  10. ↑ Nicastro, G. (May 2003). Franzoni, L.; de Chiara, C.; Mancin, A. C.; Giglio, J. R.; Spisni, A. "Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom". Eur. J. Biochem. 270 (9): 1969–1979. doi: 10.1046/j.1432-1033.2003.03563.x . PMID   12709056. S2CID   20601072.
  11. ↑ Griffin, P. R.; Aird, S. D. (1990). "A new small myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis)". FEBS Letters. 274 (1): 43–47. doi: 10.1016/0014-5793(90)81325-I . PMID   2253781. S2CID   45019479.
  12. ↑ Samejima, Y.; Aoki, Y.; Mebs, D. (1991). "Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus)". Toxicon. 29 (4): 461–468. doi:10.1016/0041-0101(91)90020-r. PMID   1862521.
  13. 1 2 Whittington, C. M.; Papenfuss, A. T.; Bansal, P.; et al. (June 2008). "Defensins and the convergent evolution of platypus and reptile venom genes". Genome Research. 18 (6): 986–094. doi:10.1101/gr.7149808. PMC   2413166 . PMID   18463304.
  14. ↑ Sobral, Filipa; Sampaio, Andreia; Falcão, Soraia; et al. (2016). "Chemical characterization, antioxidant, anti-inflammatory and cytotoxic properties of bee venom collected in Northeast Portugal" (PDF). Food and Chemical Toxicology. 94: 172–177. doi:10.1016/j.fct.2016.06.008. hdl:10198/13492. PMID   27288930. S2CID   21796492.
  15. ↑ Peng, Xiaozhen; Dai, Zhipan; Lei, Qian; et al. (April 2017). "Cytotoxic and apoptotic activities of black widow spiderling extract against HeLa cells". Experimental and Therapeutic Medicine. 13 (6): 3267–3274. doi:10.3892/etm.2017.4391. PMC   5450530 . PMID   28587399.
  16. ↑ Post Downing, Jeanne (1983). "Venom: Source of a Sex Pheromone in the Social Wasp Polistes fuscatus (Hymenoptera: Vespidae)". Journal of Chemical Ecology. 9 (2): 259–266. Bibcode:1983JCEco...9..259P. doi:10.1007/bf00988043. PMID   24407344. S2CID   32612635.
  17. ↑ Post Downing, Jeanne (1984). "Alarm response to venom by social wasps Polistes exclamans and P. fuscatus". Journal of Chemical Ecology. 10 (10): 1425–1433. doi:10.1007/BF00990313. PMID   24318343. S2CID   38398672.
  18. ↑ Baracchi, David (January 2012). "From individual to collective immunity: The role of the venom as antimicrobial agent in the Stenogastrinae wasp societies". Journal of Insect Physiology. 58 (1): 188–193. doi:10.1016/j.jinsphys.2011.11.007. hdl: 2158/790328 . PMID   22108024. S2CID   206185438.
  19. ↑ Pinto, Antônio F. M.; Berger, Markus; Reck, José; Terra, Renata M. S.; Guimarães, Jorge A. (15 December 2010). "Lonomia obliqua venom: In vivo effects and molecular aspects associated with the hemorrhagic syndrome". Toxicon. 56 (7): 1103–1112. doi:10.1016/j.toxicon.2010.01.013. PMID   20114060.
  20. ↑ Touchard, Axel; Aili, Samira; Fox, Eduardo; et al. (20 January 2016). "The Biochemical Toxin Arsenal from Ant Venoms". Toxins. 8 (1): 30. doi: 10.3390/toxins8010030 . ISSN   2072-6651. PMC   4728552 . PMID   26805882.
  21. ↑ 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. 65 (12): 2319–2327. doi:10.1007/s00265-011-1242-y. S2CID   23234351.
  22. ↑ Frost, Emily (30 August 2013). "What's Behind That Jellyfish Sting?". Smithsonian. Retrieved 30 September 2018.
  23. ↑ Bonamonte, Domenico; Angelini, Gianni (2016). Aquatic Dermatology: Biotic, Chemical and Physical Agents. Springer International. pp. 54–56. ISBN   978-3-319-40615-2.
  24. ↑ Gallagher, Scott A. (2 August 2017). "Echinoderm Envenomation". EMedicine. Retrieved 12 October 2010.
  25. ↑ Olivera, B. M.; Teichert, R. W. (2007). "Diversity of the neurotoxic Conus peptides: a model for concerted pharmacological discovery". Molecular Interventions. 7 (5): 251–260. doi:10.1124/mi.7.5.7. PMID   17932414.
  26. ↑ Barry, Carolyn (17 April 2009). "All Octopuses Are Venomous, Study Says". National Geographic . Archived from the original on 30 September 2018. Retrieved 30 September 2018.
  27. 1 2 3 Smith, William Leo; Wheeler, Ward C. (2006). "Venom Evolution Widespread in Fishes: A Phylogenetic Road Map for the Bioprospecting of Piscine Venoms". Journal of Heredity. 97 (3): 206–217. doi: 10.1093/jhered/esj034 . PMID   16740627.
  28. ↑ Venomous Amphibians (Page 1) – Reptiles (Including Dinosaurs) and Amphibians – Ask a Biologist Q&A. Askabiologist.org.uk. Retrieved on 2013-07-17.
  29. ↑ 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. JSTOR   1443606.
  30. ↑ Jared, Carlos; Mailho-Fontana, Pedro Luiz; Antoniazzi, Marta Maria; et al. (17 August 2015). "Venomous Frogs Use Heads as Weapons". Current Biology. 25 (16): 2166–2170. Bibcode:2015CBio...25.2166J. doi: 10.1016/j.cub.2015.06.061 . ISSN   0960-9822. PMID   26255851. S2CID   13606620.
  31. ↑ Bauchot, Roland (1994). Snakes: A Natural History. Sterling. pp. 194–209. ISBN   978-1-4027-3181-5.
  32. ↑ "Snake Bites". A. D. A. M. Inc. 16 October 2017. Retrieved 30 September 2018.
  33. ↑ Hargreaves, Adam D.; Swain, Martin T.; Hegarty, Matthew J.; Logan, Darren W.; Mulley, John F. (30 July 2014). "Restriction and Recruitment—Gene Duplication and the Origin and Evolution of Snake Venom Toxins". Genome Biology and Evolution. 6 (8): 2088–2095. doi:10.1093/gbe/evu166. PMC   4231632 . PMID   25079342.
  34. ↑ Daltry, Jennifer C.; Wuester, Wolfgang; Thorpe, Roger S. (1996). "Diet and snake venom evolution". Nature. 379 (6565): 537–540. Bibcode:1996Natur.379..537D. doi:10.1038/379537a0. PMID   8596631. S2CID   4286612.
  35. ↑ Cantrell, F. L. (2003). "Envenomation by the Mexican beaded lizard: a case report". Journal of Toxicology. Clinical Toxicology. 41 (3): 241–244. doi:10.1081/CLT-120021105. PMID   12807305. S2CID   24722441.
  36. 1 2 3 Mullin, Emily (29 November 2015). "Animal Venom Database Could Be Boon To Drug Development". Forbes. Retrieved 30 September 2018.
  37. 1 2 Fry, B. G.; Wroe, S.; Teeuwisse, W. (June 2009). "A central role for venom in predation by Varanus komodoensis (Komodo Dragon) and the extinct giant Varanus (Megalania) priscus". PNAS. 106 (22): 8969–8974. Bibcode:2009PNAS..106.8969F. doi: 10.1073/pnas.0810883106 . PMC   2690028 . PMID   19451641.
  38. ↑ Fry, B. G.; Wuster, W.; Ramjan, S. F. R.; Jackson, T.; Martelli, P.; Kini, R. M. 2003c. Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: Evolutionary and toxinological implications. Rapid Communications in Mass Spectrometry 17:2047-2062.
  39. ↑ Fry, B. G.; Vidal, N.; Norman, J. A.; et al. (February 2006). "Early evolution of the venom system in lizards and snakes". Nature. 439 (7076): 584–588. Bibcode:2006Natur.439..584F. doi:10.1038/nature04328. PMID   16292255. S2CID   4386245.
  40. ↑ Benoit, J.; Norton, L. A.; Manger, P. R.; Rubidge, B. S. (2017). "Reappraisal of the envenoming capacity of Euchambersia mirabilis (Therapsida, Therocephalia) using μCT-scanning techniques". PLOS ONE. 12 (2): e0172047. Bibcode:2017PLoSO..1272047B. doi: 10.1371/journal.pone.0172047 . PMC   5302418 . PMID   28187210.
  41. ↑ Nekaris, K. Anne-Isola; Moore, Richard S.; Rode, E. Johanna; Fry, Bryan G. (27 September 2013). "Mad, bad and dangerous to know: the biochemistry, ecology and evolution of slow loris venom". Journal of Venomous Animals and Toxins Including Tropical Diseases. 19 (1): 21. doi: 10.1186/1678-9199-19-21 . PMC   3852360 . PMID   24074353.
  42. ↑ Ligabue-Braun, R.; Verli, H.; Carlini, C. R. (2012). "Venomous mammals: a review". Toxicon. 59 (7–8): 680–695. doi:10.1016/j.toxicon.2012.02.012. PMID   22410495.
  43. ↑ Jørn H. Hurum, Zhe-Xi Luo, and Zofia Kielan-Jaworowska, Were mammals originally venomous?, Acta Palaeontologica Polonica 51 (1), 2006: 1-11
  44. ↑ Wong, E. S.; Belov, K. (2012). "Venom evolution through gene duplications". Gene. 496 (1): 1–7. doi:10.1016/j.gene.2012.01.009. PMID   22285376.
  45. ↑ GBD 2013 Mortality and Causes of Death Collaborators (17 December 2014). "Global, regional, and national age-sex specific all-cause and cause-specific mortality for 240 causes of death, 1990-2013: a systematic analysis for the Global Burden of Disease Study 2013". Lancet. 385 (9963): 117–171. doi:10.1016/S0140-6736(14)61682-2. PMC   4340604 . PMID   25530442.
  46. ↑ Pal, S. K.; Gomes, A.; Dasgupta, S. C.; Gomes, A. (2002). "Snake venom as therapeutic agents: from toxin to drug development". Indian Journal of Experimental Biology. 40 (12): 1353–1358. PMID   12974396.
  47. ↑ Holland, Jennifer S. (February 2013). "The Bite That Heals". National Geographic . Archived from the original on 25 May 2018. Retrieved 30 September 2018.
  48. ↑ Fox, Eduardo G.P.; Xu, Meng; Wang, Lei; Chen, Li; Lu, Yong-Yue (May 2018). "Speedy milking of fresh venom from aculeate hymenopterans". Toxicon. 146: 120–123. doi:10.1016/j.toxicon.2018.02.050. PMID   29510162.
  49. ↑ Fox, Eduardo Gonçalves Paterson (2021). "Venom Toxins of Fire Ants". In Gopalakrishnakone, P.; Calvete, Juan J. (eds.). Venom Genomics and Proteomics. Springer Netherlands. pp. 149–167. doi:10.1007/978-94-007-6416-3_38. ISBN   9789400766495.
  50. ↑ Calvete, Juan J. (December 2013). "Snake venomics: From the inventory of toxins to biology". Toxicon. 75: 44–62. doi:10.1016/j.toxicon.2013.03.020. ISSN   0041-0101. PMID   23578513.
  51. ↑ Arbuckle, Kevin; Rodríguez de la Vega, Ricardo C.; Casewell, Nicholas R. (December 2017). "Coevolution takes the sting out of it: Evolutionary biology and mechanisms of toxin resistance in animals" (PDF). Toxicon. 140: 118–131. doi:10.1016/j.toxicon.2017.10.026. PMID   29111116. S2CID   11196041.
  52. ↑ Dawkins, Richard; Krebs, John Richard; Maynard Smith, J.; Holliday, Robin (21 September 1979). "Arms races between and within species". Proceedings of the Royal Society of London. Series B. Biological Sciences. 205 (1161): 489–511. Bibcode:1979RSPSB.205..489D. doi:10.1098/rspb.1979.0081. PMID   42057. S2CID   9695900.
  53. ↑ McCabe, Thomas M.; Mackessy, Stephen P. (2015). Gopalakrishnakone, P.; Malhotra, Anita (eds.). Evolution of Resistance to Toxins in Prey. Toxinology. Springer Netherlands. pp. 1–19. doi:10.1007/978-94-007-6727-0_6-1. ISBN   978-94-007-6727-0.{{cite book}}: |work= ignored (help)
  54. ↑ Nuismer, Scott L.; Ridenhour, Benjamin J.; Oswald, Benjamin P. (2007). "Antagonistic Coevolution Mediated by Phenotypic Differences Between Quantitative Traits". Evolution. 61 (8): 1823–1834. doi: 10.1111/j.1558-5646.2007.00158.x . PMID   17683426. S2CID   24103.
  55. 1 2 Holding, Matthew L.; Drabeck, Danielle H.; Jansa, Sharon A.; Gibbs, H. Lisle (1 November 2016). "Venom Resistance as a Model for Understanding the Molecular Basis of Complex Coevolutionary Adaptations". Integrative and Comparative Biology. 56 (5): 1032–1043. doi: 10.1093/icb/icw082 . ISSN   1540-7063. PMID   27444525.
  56. ↑ Calvete, Juan J. (1 March 2017). "Venomics: integrative venom proteomics and beyond". Biochemical Journal. 474 (5): 611–634. doi:10.1042/BCJ20160577. ISSN   0264-6021. PMID   28219972.
  57. ↑ Morgenstern, David; King, Glenn F. (1 March 2013). "The venom optimization hypothesis revisited". Toxicon. 63: 120–128. doi:10.1016/j.toxicon.2012.11.022. PMID   23266311.
  58. ↑ Poran, Naomie S.; Coss, Richard G.; Benjamini, Eli (1 January 1987). "Resistance of California ground squirrels (Spermophilus Beecheyi) to the venom of the northern Pacific rattlesnake (Crotalus Viridis Oreganus): A study of adaptive variation". Toxicon. 25 (7): 767–777. doi:10.1016/0041-0101(87)90127-9. ISSN   0041-0101. PMID   3672545.
  59. ↑ Coss, Richard G.; Poran, Naomie S.; Gusé, Kevin L.; Smith, David G. (1 January 1993). "Development of Antisnake Defenses in California Ground Squirrels (Spermophilus Beecheyi): II. Microevolutionary Effects of Relaxed Selection From Rattlesnakes". Behaviour. 124 (1–2): 137–162. doi:10.1163/156853993X00542. ISSN   0005-7959.
  60. ↑ Holding, Matthew L.; Biardi, James E.; Gibbs, H. Lisle (27 April 2016). "Coevolution of venom function and venom resistance in a rattlesnake predator and its squirrel prey". Proceedings of the Royal Society B: Biological Sciences. 283 (1829): 20152841. doi:10.1098/rspb.2015.2841. PMC   4855376 . PMID   27122552.
  61. ↑ Conant, Roger (1975). A field guide to reptiles and amphibians of Eastern and Central North America (Second ed.). Boston: Houghton Mifflin. ISBN   0-395-19979-4. OCLC   1423604.
  62. ↑ Weinstein, Scott A.; DeWitt, Clement F.; Smith, Leonard A. (December 1992). "Variability of Venom-Neutralizing Properties of Serum from Snakes of the Colubrid Genus Lampropeltis". Journal of Herpetology. 26 (4): 452. doi:10.2307/1565123. JSTOR   1565123. S2CID   53706054.
  63. ↑ Heatwole, Harold; Poran, Naomie S. (15 February 1995). "Resistances of Sympatric and Allopatric Eels to Sea Snake Venoms". Copeia. 1995 (1): 136. doi:10.2307/1446808. JSTOR   1446808.
  64. ↑ Heatwole, Harold; Powell, Judy (May 1998). "Resistance of eels (Gymnothorax) to the venom of sea kraits (Laticauda colubrina): a test of coevolution". Toxicon. 36 (4): 619–625. doi:10.1016/S0041-0101(97)00081-0. PMID   9643474.
  65. ↑ Zimmerman, K. D.; Heatwole, Harold; Davies, H. I. (1 March 1992). "Survival times and resistance to sea snake (Aipysurus laevis) venom by five species of prey fish". Toxicon. 30 (3): 259–264. doi:10.1016/0041-0101(92)90868-6. ISSN   0041-0101. PMID   1529461.
  66. ↑ Litsios, Glenn; Sims, Carrie A.; Wüest, Rafael O.; Pearman, Peter B.; Zimmermann, Niklaus E.; Salamin, Nicolas (2 November 2012). "Mutualism with sea anemones triggered the adaptive radiation of clownfishes". BMC Evolutionary Biology. 12 (1): 212. Bibcode:2012BMCEE..12..212L. doi: 10.1186/1471-2148-12-212 . ISSN   1471-2148. PMC   3532366 . PMID   23122007.
  67. ↑ Fautin, Daphne G. (1991). "The anemonefish symbiosis: what is known and what is not". Symbiosis. 10: 23–46 – via University of Kansas.
  68. ↑ Mebs, Dietrich (15 December 2009). "Chemical biology of the mutualistic relationships of sea anemones with fish and crustaceans". Toxicon. Cnidarian Toxins and Venoms. 54 (8): 1071–1074. doi:10.1016/j.toxicon.2009.02.027. ISSN   0041-0101. PMID   19268681.
  69. ↑ da Silva, Karen Burke; Nedosyko, Anita (2016), Goffredo, Stefano; Dubinsky, Zvy (eds.), "Sea Anemones and Anemonefish: A Match Made in Heaven", The Cnidaria, Past, Present and Future: The world of Medusa and her sisters, Springer International Publishing, pp. 425–438, doi:10.1007/978-3-319-31305-4_27, ISBN   978-3-319-31305-4
  70. ↑ Nedosyko, Anita M.; Young, Jeanne E.; Edwards, John W.; Silva, Karen Burke da (30 May 2014). "Searching for a Toxic Key to Unlock the Mystery of Anemonefish and Anemone Symbiosis". PLOS ONE. 9 (5): e98449. Bibcode:2014PLoSO...998449N. doi: 10.1371/journal.pone.0098449 . ISSN   1932-6203. PMC   4039484 . PMID   24878777.
  71. ↑ Mebs, D. (1 September 1994). "Anemonefish symbiosis: Vulnerability and resistance of fish to the toxin of the sea anemone". Toxicon. 32 (9): 1059–1068. doi:10.1016/0041-0101(94)90390-5. ISSN   0041-0101. PMID   7801342.
  72. ↑ Lubbock, R.; Smith, David Cecil (13 February 1980). "Why are clownfishes not stung by sea anemones?". Proceedings of the Royal Society of London. Series B. Biological Sciences. 207 (1166): 35–61. Bibcode:1980RSPSB.207...35L. doi:10.1098/rspb.1980.0013. S2CID   86114704.
  73. 1 2 Litsios, Glenn; Kostikova, Anna; Salamin, Nicolas (22 November 2014). "Host specialist clownfishes are environmental niche generalists". Proceedings of the Royal Society B: Biological Sciences. 281 (1795): 20133220. doi:10.1098/rspb.2013.3220. PMC   4213602 . PMID   25274370.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.