Isolation and characterization of a novel postsynaptic/cytotoxic neurotoxin from <i>Daboia russelli russelli</i> venom

Shelke, R. R. J.; Sathish, S.; Gowda, T. Veerabasappa

doi:10.1034/j.1399-3011.2002.02969.x

Cited by 22 publications

(19 citation statements)

References 26 publications

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“…In fact we also observed other clusters in our database matching the same 3FTx gene segment from Bungarus multicinctus, but they seem not to code a polypeptide. Other reports of postsynaptic 3FTx neurotoxins in Viperidae are based only on immuno or pharmacological evidences ( Jiang et al 1987) and do not describe sequences, excepted by a N terminus of a possible 3FTx from Daboia russelli (Shelke et al 2002).…”

Section: Discussionmentioning

confidence: 99%

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

et al. 2006

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Efforts to describe toxins from the two major families of venomous snakes (Viperidae and Elapidae) usually reveal proteins belonging to few structural types, particular of each family. Here we carried on an effort to determine uncommon cDNAs that represent possible new toxins from Lachesis muta (Viperidae). In addition to nine classes of typical toxins, atypical molecules never observed in the hundreds of Viperidae snakes studied so far are highly expressed: a diverging C-type lectin that is related to Viperidae toxins but appears to be independently originated; an ohanin-like toxin, which would be the third member of the most recently described class of Elapidae toxins, related to human butyrophilin and B30.2 proteins; and a 3FTx-like toxin, a new member of the widely studied three-finger family of proteins, which includes major Elapidae neurotoxins and CD59 antigen. The presence of these common and uncommon molecules suggests that the repertoire of toxins could be more conserved between families than has been considered, and their features indicate a dynamic process of venom evolution through molecular mechanisms, such as multiple recruitments of important scaffolds and domain exchange between paralogs, always keeping a minimalist nature in most toxin structures in opposition to their nontoxin counterparts.

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Section: Discussionmentioning

confidence: 99%

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

et al. 2006

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“…[11][12][13][14] The N-terminal sequence, molecular mass, and pharmacological activities of the Daboia russelli venom 3FTx indicate that it is a short-chain neurotoxin such as that found in Elapid venom. 43 On the other hand, the colubrid 3FTx (termed denmotoxin) represents a bird-specific neu- 1 2 XYCFWSPGSR a X, Ile or Leu; Z, pyrrolidone carboxylic acid; M(ox), methionine sulfoxide. Unless otherwise stated, for MS/MS analyses, cysteine residues were carbamidomethylated.…”

Section: Large Venom Toxin Composition Variation Betweenmentioning

confidence: 99%

Snake Venomics of Central American Pitvipers: Clues for Rationalizing the Distinct Envenomation Profiles of Atropoides nummifer and Atropoides picadoi

et al. 2007

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We report the proteomic characterization of the Central American pitvipers Atropoides nummifer and Atropoides picadoi. The crude venoms were fractionated by reverse-phase high-performance liquid chromatography (HPLC), followed by analysis of each chromatographic fraction by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), N-terminal sequencing, matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass fingerprinting, and collision-induced dissociation-tandem mass spectrometry (CID-MS/MS) of tryptic peptides. Each venom contained a number of bradykinin-potentiating peptides and around 25-27 proteins of molecular masses in the range of 7-112 kDa, belonging to only nine different toxin families (disintegrin, DC fragment, snake venom vascular endothelial growth factor, phospholipases A2, serine protease, cysteine-rich secretory proteins, C-type lectins, L-amino acid oxidase, and Zn2+-dependent metalloproteases), albeit distinctly distributed among the two Atropoides species. In addition, A. nummifer expresses low amounts of a three-finger toxin not detected in the venom of A. picadoi. The major toxins of A. nummifer belong to the PLA2 (relative abundance, 36.5%) and the serine proteinase (22%) families, whereas the most abundant A. picadoi toxins are Zn2+-dependent metalloproteinases (66.4%). We estimate that the similarity of venom proteins between the two Atropoides taxa may be around 14-16%. The high degree of differentiation in the venom proteome among congeneric taxa emphasizes unique aspects of venom composition of related species of Atropoides snakes and points to a strong role for adaptive diversification via natural selection as a cause of this distinctiveness. On the other hand, their distinct venom toxin compositions provide clues for rationalizing the low hemorrhagic, coagulant, and defibrinating activities and the high myotoxic and proteolytic effects evoked by A. nummifer snakebite in comparison to other crotaline snake venoms and the high hemorrhagic activity of A. picadoi.

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“…Snake venoms do not contain a homogenous single toxin, but are complex cocktails of enzymes, polypeptides, non-enzymatic proteins, nucleotides, and other substances, many of which may have different neurotoxic properties [91], [112], [113], [116], [134], [145], [146] (Table 2). The studies of Chang and others of the Chinese (or formerly Formosan) cobra ( Naja atra ) venom (1966, 1972) [138], [139] highlighted the complexity of multiple actions of different neurotoxins in the same venom.…”

Section: Snake Venom and Neuromuscular Blockmentioning

confidence: 99%

“…For example, a post-synaptic toxin (DNTx-I—Daboia Neurotoxin 1) has been isolated from the venom of Russell's viper ( Daboia russelii ) [146], in addition to the well-known pre-synaptic PLA2 toxin [147], [148]. Venom of kraits ( Bungarus spp.)…”

Section: Snake Venom and Neuromuscular Blockmentioning

confidence: 99%

Neurotoxicity in Snakebite—The Limits of Our Knowledge

2013

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Snakebite is classified by the WHO as a neglected tropical disease. Envenoming is a significant public health problem in tropical and subtropical regions. Neurotoxicity is a key feature of some envenomings, and there are many unanswered questions regarding this manifestation. Acute neuromuscular weakness with respiratory involvement is the most clinically important neurotoxic effect. Data is limited on the many other acute neurotoxic manifestations, and especially delayed neurotoxicity. Symptom evolution and recovery, patterns of weakness, respiratory involvement, and response to antivenom and acetyl cholinesterase inhibitors are variable, and seem to depend on the snake species, type of neurotoxicity, and geographical variations. Recent data have challenged the traditional concepts of neurotoxicity in snake envenoming, and highlight the rich diversity of snake neurotoxins. A uniform system of classification of the pattern of neuromuscular weakness and models for predicting type of toxicity and development of respiratory weakness are still lacking, and would greatly aid clinical decision making and future research. This review attempts to update the reader on the current state of knowledge regarding this important issue.

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Isolation and characterization of a novel postsynaptic/cytotoxic neurotoxin from Daboia russelli russelli venom

Cited by 22 publications

References 26 publications

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

Snake Venomics of Central American Pitvipers: Clues for Rationalizing the Distinct Envenomation Profiles of Atropoides nummifer and Atropoides picadoi

Neurotoxicity in Snakebite—The Limits of Our Knowledge

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