Venom of the Brown Treesnake, Boiga irregularis: Ontogenetic shifts and taxa-specific toxicity

Mackessy, Stephen P.; Sixberry, Nicole M.; Heyborne, William H.; Fritts, Thomas H.

doi:10.1016/j.toxicon.2006.01.007

Cited by 181 publications

(138 citation statements)

References 41 publications

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“…Thus, although the results indicated that the major PLA 2 eluted in peak 9 (which accounts for ~20% of the total venom proteins) was not lethal to mice, the possibility that this protein exhibits taxon-specific activity, as reported for other toxins [83][84][85][86][87], requires future detailed investigation. Finally, of relevance from a clinical standpoint, the sea snake antivenom manufactured by CSL in Australia using the venom of E. schistosa displays sufficient immunological cross-reactivity to provide protection from the lethal effects of P.…”

Section: Accepted M Manuscriptmentioning

confidence: 80%

Two color morphs of the pelagic yellow-bellied sea snake, Pelamis platura, from different locations of Costa Rica: Snake venomics, toxicity, and neutralization by antivenom

Lomonte

Plá

Sasa

et al. 2014

Journal of Proteomics

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Section: Accepted M Manuscriptmentioning

confidence: 80%

Two color morphs of the pelagic yellow-bellied sea snake, Pelamis platura, from different locations of Costa Rica: Snake venomics, toxicity, and neutralization by antivenom

Lomonte

Plá

Sasa

et al. 2014

Journal of Proteomics

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“…Snakes from the Boiga sp. mainly feed on the nonmammalian prey such as birds (12,13,60), whereas elapids, including the king cobra, mainly prey on snakes and rodents and only occasionally and opportunistically on birds (61,62). Venom compositions of snakes are known to be dependent on prey specificity to ensure efficiency in their capture and killing (58).…”

Section: Discussionmentioning

confidence: 99%

Structural and Functional Characterization of a Novel Homodimeric Three-finger Neurotoxin from the Venom of Ophiophagus hannah (King Cobra)

Roy

Zhou

Chong

et al. 2010

Journal of Biological Chemistry

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Snake venoms are a mixture of pharmacologically active proteins and polypeptides that have led to the development of molecular probes and therapeutic agents. Here, we describe the structural and functional characterization of a novel neurotoxin, haditoxin, from the venom of Ophiophagus hannah (King cobra). Haditoxin exhibited novel pharmacology with antagonism toward muscle (␣␤␥␦) and neuronal (␣ 7 , ␣ 3 ␤ 2 , and ␣ 4 ␤ 2 ) nicotinic acetylcholine receptors (nAChRs) with highest affinity for ␣ 7 -nAChRs. The high resolution (1.5 Å ) crystal structure revealed haditoxin to be a homodimer, like -neurotoxins, which target neuronal ␣ 3 ␤ 2 -and ␣ 4 ␤ 2 -nAChRs. Interestingly however, the monomeric subunits of haditoxin were composed of a three-finger protein fold typical of curaremimetic shortchain ␣-neurotoxins. Biochemical studies confirmed that it existed as a non-covalent dimer species in solution. Its structural similarity to short-chain ␣-neurotoxins and -neurotoxins notwithstanding, haditoxin exhibited unique blockade of ␣ 7 -nAChRs (IC 50 180 nM), which is recognized by neither shortchain ␣-neurotoxins nor -neurotoxins. This is the first report of a dimeric short-chain ␣-neurotoxin interacting with neuronal ␣ 7 -nAChRs as well as the first homodimeric three-finger toxin to interact with muscle nAChRs.Snake venoms are a rich source of pharmacologically active proteins and polypeptides targeting a variety of receptors with high affinity and specificity (1). Because of their high specificity, some of these molecules have contributed significantly (a) to the isolation and characterization of different receptors and their subtypes in the field of molecular pharmacology and (b) as lead compounds in the development of therapeutic agents (2, 3). For example, the discovery of ␣-bungarotoxin, a postsynaptic neurotoxin from the venom of Bungarus multicinctus, led to the identification of the nicotinic acetylcholine receptor (nAChR), 3 the first isolated receptor protein (4) as well as the first one to be characterized electrophysiologically (5) and biochemically (6, 7). Subsequently, it was also used to characterize several other nAChRs (8 -10).Snake venom proteins can be broadly classified as enzymatic and non-enzymatic proteins. Three-finger toxins (3FTxs) are the largest group of non-enzymatic snake venom proteins (1, 11). They are most commonly found in the venoms of elapid and hydrophiid snakes. Recently, our laboratory has also demonstrated the presence of 3FTxs from colubrid venoms (12, 13), and 3FTx transcripts have been found in the venom gland transcriptome of viperid snakes (14, 15). The proteins in this family of toxins share a common structural scaffold of three ␤-sheeted loops emerging from a central core (11,16). Despite the overall similarity in structure, these proteins have diverse functional properties. Members of this family include neurotoxins targeting the cholinergic system (7, 11, 16), cytotoxins/cardiotoxins interacting with the cell membranes (17), calciseptine and related toxins that block th...

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“…Lately, 2DE has been the preferred technique used by several researchers to decipher the complexity of venoms due to its capability of separating a mixture of proteins based on two parameters, pI and MW (15)(16)(17)(18)(19). Owing to the close proximity of molecular weights among toxins bearing different net charges, SDS-PAGE was not able to provide efficient differentiation (6).…”

Section: Discussionmentioning

confidence: 99%

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Vejayan¹,

Yee²,

Ponnudurai³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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Snake venoms comprise a highly complex mixture of proteins, which requires for their characterization the use of versatile two-dimensional electrophoresis techniques. In the present study, venoms obtained from eight snakes (Ophiophagus hannah, Naja kaouthia, Naja sumatrana, Bungarus fasciatus, Trimeresurus sumatranus, Tropidolaemus wagleri, Enhydrina schistosa and Calloselasma rhodostoma) commonly found in Malaysia were separated based on two independent properties, isoelectric point (pI) and molecular weight (MW). Many differences in snake venoms at the inter-family, inter-subfamily, inter-genus and inter-species levels were revealed. Notably, proteins from individuals of the Viperidae family -Trimeresurus sumatranus, Tropidolaemus wagleri and Calloselasma rhodostoma -were found to be numerous and scattered by the two-dimensional gel electrophoresis (2DE) specifically in regions between 37 and 100 kDa compared to the Elapidae venom proteins. The latter were clustered at the basic and lower molecular mass region (less than 20 kDa). Trains of spots were commonly observed, indicating that these proteins may be derived from post-translational modifications. Ophiophagus hannah (Elapidae) revealed a great amount of protein spots in the higher molecular mass range when compared to Enhydrina schistosa, Naja kaouthia, Naja sumatrana and Bungarus fasciatus. Overall 2DE showed large differences in the venom profile of each species, which might be employed as an ancillary tool to the identification of venomous snake species.

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Venom of the Brown Treesnake, Boiga irregularis: Ontogenetic shifts and taxa-specific toxicity

Cited by 181 publications

References 41 publications

Two color morphs of the pelagic yellow-bellied sea snake, Pelamis platura, from different locations of Costa Rica: Snake venomics, toxicity, and neutralization by antivenom

Two color morphs of the pelagic yellow-bellied sea snake, Pelamis platura, from different locations of Costa Rica: Snake venomics, toxicity, and neutralization by antivenom

Structural and Functional Characterization of a Novel Homodimeric Three-finger Neurotoxin from the Venom of Ophiophagus hannah (King Cobra)

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

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