Tropidolaemus wagleri

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Tropidolaemus wagleri
Tropidolaemus wagleri, Wagler's palm pit viper - Takua Pa District, Phang-nga Province (48238132136).jpg
Scientific classification OOjs UI icon edit-ltr.svg
Domain: Eukaryota
Kingdom: Animalia
Phylum: Chordata
Class: Reptilia
Order: Squamata
Suborder: Serpentes
Family: Viperidae
Genus: Tropidolaemus
Species:
T. wagleri
Binomial name
Tropidolaemus wagleri
(F. Boie, 1827)
Synonyms [2]
  • C[ophias]. Wagleri
    H. Boie, 1826
    (nomen nudum)
  • [Cophias] Wagleri
    F. Boie, 1827
    (nomen conservandum)
  • Tropidolaemus wagleri
    Wagler, 1830
  • Trigonoc[ephalus]. wagleri
    Schlegel, 1837
  • Trimesurus maculatus
    Gray, 1842
  • Trimesurus Philippensis
    Gray, 1842
  • Trimesurus subannulatus
    Gray, 1842
  • Trigonocephalus Wagleri var. Celebensis
    Gray, 1849
  • Trigonocephalus Wagleri var. Sumatrensis
    Gray, 1849
  • Tropidolaemus hombronii
    Guichenot In Jacquinot & Guichenot, 1853
  • Tropidolaemus wagleri
    A.M.C. Duméril, Bibron &
    A.H.A. Duméril, 1854
  • Tropidolaemus hombroni
    — A.M.C. Duméril, Bibron &
    A.H.A. Duméril, 1854
  • Tropidolaemus Schlegelii
    Bleeker, 1857
  • T[rigonocephalus]. Hombroni
    Jan, 1859
  • Tropidolaemus Philippensis
    W. Peters, 1861
  • Tropidolaemus subannulatus
    — W. Peters, 1861
  • Trimeresurus wagleri
    Günther, 1864
  • Tropidolaemus Schlegeli
    Theobald, 1868
  • Tropidolaemus subannulatus var. celebensis
    — W. Peters, 1872
  • Tropidolaemus subannulatus var. immaculatus
    W. Peters, 1872
  • Bothrops Wagleri
    F. Müller, 1880
  • Lachesis wagleri
    Boulenger, 1896
  • Trimeresurus wagleri alboviridis
    Taylor, 1917
  • Trimeresurus philippensis
    — Taylor, 1922
  • Trimeresurus wagleri wagleri
    — Taylor, 1922
  • Trimeresurus wagleri philippensis
    — Taylor, 1922
  • Trimeresurus wagleri subannulatus
    — Taylor, 1922
  • [Bothrops] philippensis
    Maslin, 1942
  • Tropidolaemus wagleri
    Hoge & Romano-Hoge, 1981
  • Tropidolaemus philippinensis
    David & Vogel, 1996
  • Trimesurus [sic] philippinensis
    — David & Vogel, 1996
    (ex errore)
  • Trimeresurus philippinensis
    — David & Vogel, 1996
  • Tropidolaemus wagleri
    — David & Vogel, 1996

Tropidolaemus wagleri, more commonly known as Wagler's pit viper, is a species of venomous snake, a pit viper in the subfamily Crotalinae of the family Viperidae. The species is endemic to Southeast Asia. There are no subspecies that are recognized as being valid. [3] It is sometimes referred to as the temple viper because of its abundance around the Temple of the Azure Cloud in Malaysia.

Contents

Etymology

The specific name, wagleri, is in honour of German herpetologist Johann Georg Wagler. [4]

Description

LachesisWagleriFullRooij.jpg

The Wagler's pit viper is sexually dimorphic: the females grow to approximately 1 m (39+14 in) in total length (including tail), their bodies being black with yellow stripes. Males, on the other hand, typically do not exceed 75 cm (29+12 in). Males have large triangular-shaped heads, with relatively thin green bodies. They are almost entirely arboreal, and their tails are prehensile to aid in climbing.

They are found in a wide variety of colors and patterns, often referred to as "phases". In the past, some researchers classified the different phases as subspecies. The phases vary greatly from having a black or brown coloration as a base, with orange and yellow banding, to others having a light green as the base color, with yellow or orange banding, and many variations therein.

Lateral view of an adult male's head. Wagler's Pit Viper Male.jpg
Lateral view of an adult male's head.

Common names

Common names for the Wagler's pit viper include temple viper, temple pit viper, [5] bamboo snake, temple snake, speckled pit viper, [6] and temple pitviper. [7]

Geographic range

A green phase of Wagler's pit viper in a terrarium of Reptile Park, Taman Mini Indonesia Indah, Jakarta, Indonesia. Wagler's Pit Viper in TMII Reptile Park.JPG
A green phase of Wagler's pit viper in a terrarium of Reptile Park, Taman Mini Indonesia Indah, Jakarta, Indonesia.

The Wagler's pit viper is found in southern Vietnam from the provinces of Minh Hai and Song Be, in southern Thailand recorded from the provinces of Phang Nga, Phuket, Pattani, Surat Thani, Nakhon Si Tammarat, Narathiwat, and Yala, probably distributed throughout the Peninsula in west Malaysia, as well as the island of Penang, in Singapore and in Indonesia on Sumatra, the islands of the Riau Archipelago, Bangka, Billiton, Nias, the Mentawai Islands (Siberut), Natuna, and Karimata. [8] In a revision by Vogel et al (2007), the Wagler's pit viper species complex was differentiated into several taxa, including the resurrection of T. subannulatus. The Western Philippine populations belong to T. subannulatus, but those from Mindanao include snakes assigned to both this species and T. philippensis. Tropidolaemus subannulatus has a wide distribution in Central Indonesia, Malaysia and Philippines, the Wagler's Pit Viper is restricted to mainland Southeast Asia, down to Sumatra and Bangka, West Indonesia." [9]

Habitat

The preferred natural habitat of the Wagler's pit viper is the forest, at altitudes from sea level to 400 m (1,300 ft). [1]

Behavior

Nocturnal and arboreal, the Wagler's pit viper appears quite sluggish, as it remains motionless for long periods of time waiting for prey to pass by. When prey does pass by, or if disturbed, it can strike quickly.

Feeding

The primary diet of the Wagler's pit viper consists of rodents, birds, and lizards. The pits, one on each side of the head between the eye and the nostril, are capable of detecting temperature difference of as little as 0.003 of a degree Celsius (0.0054 of a degree Fahrenheit). [10]

Reproduction

Sexually mature females of the Wagler's pit viper bear live young by ovoviviparity. Litter size varies from 15 to 41. [11]

Venom

The venom of the Wagler's pit viper contains four novel peptides (Waglerins 1-4). The Waglerins produce fatal respiratory paralysis of adult mice. [12] [13] An initial study indicated that micromolar concentrations of Waglerin 1 act both pre- and postsynaptically to inhibit transmission across rat neuromuscular junctions. [14] However, Waglerin-1 is a more potent inhibitor of transmission across the mouse neuromuscular junction. [15] A subsequent study demonstrated that Waglerin-1 inhibited the adult mouse endplate response to acetylcholine with an IC50 of 50 nanomolar. In striking contrast, transmission across neuromuscular junctions of neonatal or transgenic mice lacking the adult acetylcholine receptor was not altered by micromolar concentrations of Waglerin-1. [16] Biochemical studies demonstrated that the exquisite selectivity of Waglerin-1 for the adult mouse acetylcholine receptor relies upon several amino acid residues unique to the epsilon subunit of the adult mouse acetylcholine receptor. [17] Waglerin-1's selectivity for the epsilon-subunit containing acetylcholine receptor of adult mice is complemented by selectivity of small peptide toxins purified from the venom of Conus geographus and Conus pergrandis for the gamma-subunit containing acetylcholine receptor of neonatal skeletal muscle. [18] [19] The Waglerins and complementary conotoxins are useful tools to discover the contribution of acetylcholine receptor subunits to synaptogenesis. [20] In addition, study of the Waglerins and related toxic peptides may lead to the discovery of novel molecular targets for drug development. While Waglerin-1 interacts with other members of the ligand-gated superfamily of ion channels, the potency is much less than for inhibition of the adult mouse muscle acetylcholine receptor. [21] [22] Structural study suggests that Waglerin-1 may undergo molecular rearrangement that allows for binding to multiple receptors. [23] The actions of Waglerin-1 reverse upon removal of the peptide.

Waglerin-1 is included in some skin creams marketed as wrinkle removers. [24] There is no scientific evidence supporting the manufacturers' suggestion that the Waglerin-1 included in their products relaxes wrinkle producing skeletal muscles.

Taxonomy

The Wagler's pit viper has undergone much taxonomic reclassification over the years and was previously placed in the genus Trimeresurus . However, its distinctly different morphology and venom characteristics set it apart, so that eventually a new genus was erected in which it was placed together with Hutton's viper, Tropidolaemus huttoni .

Related Research Articles

<span class="mw-page-title-main">Acetylcholine receptor</span> Integral membrane protein

An acetylcholine receptor is an integral membrane protein that responds to the binding of acetylcholine, a neurotransmitter.

<span class="mw-page-title-main">Neuromuscular junction</span> Junction between the axon of a motor neuron and a muscle fiber

A neuromuscular junction is a chemical synapse between a motor neuron and a muscle fiber.

<span class="mw-page-title-main">Nicotinic acetylcholine receptor</span> Acetylcholine receptors named for their selective binding of nicotine

Nicotinic acetylcholine receptors, or nAChRs, are receptor polypeptides that respond to the neurotransmitter acetylcholine. Nicotinic receptors also respond to drugs such as the agonist nicotine. They are found in the central and peripheral nervous system, muscle, and many other tissues of many organisms. At the neuromuscular junction they are the primary receptor in muscle for motor nerve-muscle communication that controls muscle contraction. In the peripheral nervous system: (1) they transmit outgoing signals from the presynaptic to the postsynaptic cells within the sympathetic and parasympathetic nervous system, and (2) they are the receptors found on skeletal muscle that receive acetylcholine released to signal for muscular contraction. In the immune system, nAChRs regulate inflammatory processes and signal through distinct intracellular pathways. In insects, the cholinergic system is limited to the central nervous system.

<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">Jean-Pierre Changeux</span> French neuroscientist (born 1936)

Jean-Pierre Changeux is a French neuroscientist known for his research in several fields of biology, from the structure and function of proteins, to the early development of the nervous system up to cognitive functions. Although being famous in biological sciences for the MWC model, the identification and purification of the nicotinic acetylcholine receptor and the theory of epigenesis by synapse selection are also notable scientific achievements. Changeux is known by the non-scientific public for his ideas regarding the connection between mind and physical brain. As put forth in his book, Conversations on Mind, Matter and Mathematics, Changeux strongly supports the view that the nervous system functions in a projective rather than reactive style and that interaction with the environment, rather than being instructive, results in the selection amongst a diversity of preexisting internal representations.

<i>Azemiops</i> Genus of snakes

Azemiopinae is a monogeneric subfamily created for the genus Azemiops that contains the viper species A. feae and A. kharini. They are commonly known as Fea's vipers. No subspecies are recognized. The first specimen was collected by Italian explorer Leonardo Fea, and was described as a new genus and new species by Boulenger in 1888. Formerly considered to be one of the most primitive vipers, molecular studies have shown that it is the sister taxon to the pit vipers, Crotalinae. It is found in the mountains of Southeast Asia, in China, southeastern Tibet, and Vietnam. Like all other vipers, they are venomous.

α-Bungarotoxin Chemical compound

α-Bungarotoxin is one of the bungarotoxins, components of the venom of the elapid Taiwanese banded krait snake. It is a type of α-neurotoxin, a neurotoxic protein that is known to bind competitively and in a relatively irreversible manner to the nicotinic acetylcholine receptor found at the neuromuscular junction, causing paralysis, respiratory failure, and death in the victim. It has also been shown to play an antagonistic role in the binding of the α7 nicotinic acetylcholine receptor in the brain, and as such has numerous applications in neuroscience research.

Bamboo snake may refer to:

<i>Tropidolaemus subannulatus</i> Species of snake

The Bornean keeled green pit viper or North Philippine temple pit viper is a venomous pit viper species native to Brunei, Indonesia, Malaysia, and the Philippines. Until 2007, this species was considered part of the Tropidolaemus wagleri species complex.

A nicotinic agonist is a drug that mimics the action of acetylcholine (ACh) at nicotinic acetylcholine receptors (nAChRs). The nAChR is named for its affinity for nicotine.

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<span class="mw-page-title-main">Cobratoxin</span> Chemical compound

α-Cobratoxin is a substance of the venom of certain Naja cobras. It is a nicotinic acetylcholine receptor (nAChR) antagonist which causes paralysis by preventing the binding of acetylcholine to the nAChR.

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

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κ-Bungarotoxin Protein neurotoxin of the bungarotoxin family

κ-Bungarotoxin is a protein neurotoxin of the bungarotoxin family that is found in the venom of the many-banded krait, a snake found in Taiwan. κ-Bungarotoxin is a high affinity antagonist of nicotinic acetylcholine receptors (nAChRs), particularly of CHRNA3; it causes a post-synaptic blockade of neurotransmission. Although there is significant variability in the clinical effects of snake bites, neuromuscular paralysis and respiratory failure are associated with krait bites.

<span class="mw-page-title-main">Three-finger toxin</span> Toxin protein

Three-finger toxins are a protein superfamily of small toxin proteins found in the venom of snakes. Three-finger toxins are in turn members of a larger superfamily of three-finger protein domains which includes non-toxic proteins that share a similar protein fold. The group is named for its common structure consisting of three beta strand loops connected to a central core containing four conserved disulfide bonds. The 3FP protein domain has no enzymatic activity and is typically between 60-74 amino acid residues long. Despite their conserved structure, three-finger toxin proteins have a wide range of pharmacological effects. Most members of the family are neurotoxins that act on cholinergic intercellular signaling; the alpha-neurotoxin family interacts with muscle nicotinic acetylcholine receptors (nAChRs), the kappa-bungarotoxin family with neuronal nAChRs, and muscarinic toxins with muscarinic acetylcholine receptors (mAChRs).

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References

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Further reading