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Agkistrodon contortrix is a species of venomous snake, a pit viper, endemic to Eastern North America; it is a member of the subfamily Crotalinae in the family Viperidae. The common name for this species is the eastern copperhead. The generic name is derived from the Greek words ancistro (hooked) and odon (tooth), or fishhook. The trivial name, or specific epithet, comes from the Latin contortus ; which is usually interpreted to reference the distorted pattern of darker bands across the snakes back, which are broad at the lateral base but "pinched" into narrow hourglass shapes in the middle at the vertebral area. Five subspecies have been recognized in the past, but recent genetic analysis shows that A. contortrix and two of the subspecies are monotypic, while Agkistrodon laticinctus and the fifth subspecies are a single distinct species.
Agkistrodon piscivorus is a species of pit viper in the subfamily Crotalinae of the family Viperidae. It is the world's only semiaquatic viper, and is native to the southeastern United States. It is the only venomous species of North America's water snakes and one of 21 venomous snakes in the United States. As an adult, it is large and capable of delivering a painful and potentially fatal bite. When threatened, it may respond by coiling its body and displaying its fangs. Individuals may bite when feeling threatened or being handled in any way. It occurs in or near water, particularly in slow-moving and shallow lakes, streams, and marshes. It is a strong swimmer and has even been seen swimming in the ocean. However, it is not fully marine, unlike true sea snakes. It has successfully colonized islands off both the Atlantic and Gulf coasts.
Agkistrodon is a genus of pit vipers found in Americas from the Southern United States to northern Costa Rica. Eight species are currently recognized, all of them monotypic and closely related. Like all pit vipers, members of the genus are venomous. Common names include: cottonmouths, copperheads, and cantils. Some varieties are known as "moccasins" or "moccasin snakes", such as Agkistrodon piscivorus, the water moccasin.
Snake venom is a highly modified saliva containing zootoxins that facilitate the immobilization and digestion of prey, and defense against threats. It is injected by unique fangs during a bite, and some species are also able to spit their venom.
Disintegrins are a family of small proteins from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion.
Deinagkistrodon is a monotypic genus created for the venomous pit viper species, D. acutus, which is endemic to Southeast Asia. No subspecies are currently recognized.
Agkistrodon taylori is a venomous pitviper species found only in northeastern Mexico. It is named in honor of American herpetologist Edward Harrison Taylor.
The western diamondback rattlesnake or Texas diamond-back is a venomous rattlesnake species found in the southwestern United States and Mexico. It is likely responsible for the majority of snakebite fatalities in northern Mexico and the greatest number of snakebites in the U.S. No subspecies are currently recognized.
Calloselasma is a monotypic genus created for a venomous pit viper species, C. rhodostoma, which is endemic to Southeast Asia from Thailand to northern Malaysia and on the island of Java. No subspecies are currently recognized.
Ablomin is a toxin present in the venom of the Japanese Mamushi snake, which blocks L-type voltage-gated calcium channels.
Piscivorin is a component of snake venom secreted by the Eastern Cottonmouth. It is a member of the cysteine-rich secretory protein (CRISP) family, which blocks voltage-dependent calcium channels.
Latisemin is a cysteine-rich secretory protein that can be isolated from the venom of the Black-banded sea krait, a sea snake indigenous to the warmer waters of the western Pacific Ocean. It is a toxin that inhibits cyclic nucleotide-gated ion channels and blocks L-type calcium channels, thereby reducing smooth muscle contraction.
Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins. They are a subgroup of the CRISP, antigen 5 and Pr-1 (CAP) protein superfamily and also contain a domain related to the ShK toxins. They are substantially implicated in the functioning of the mammalian reproductive system. CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels.
Venombin A is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin I is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction
Fibrolase is an enzyme. This enzyme catalyses the following chemical reaction
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. The evolution of venom is thought to be responsible for the enormous expansion of snakes across the globe.
Snakebite envenomation is considered a public health problem in Latin America, with an estimated 70,000 cases annually, but due to underreporting, these numbers may be even higher.
References
- ↑ "MEROPS - the Peptidase Database". www.ebi.ac.uk.
- ↑ Gong, Weimin; Zhu, Xueyong; Liu, Sijiu; Teng, Maikun; Niu, Liwen (1998). "Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus". Journal of Molecular Biology. 283 (3): 657–668. doi:10.1006/jmbi.1998.2110. PMID 9784374.
