Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: evolutionary and toxinological implications

Fry, Bryan G.; Wüster, Wolfgang; Ramjan, S. F. Ryan; Martelli, Paolo; Kini, R. Manjunatha

doi:10.1002/rcm.1148

Cited by 153 publications

(116 citation statements)

References 48 publications

(79 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Proteomic analyses revealed that the venom of this widely distributed sea snake presents a relatively simple composition, including three major types of components that belong to the 3FTx, PLA 2 , and CRISP protein families, respectively. This finding seems to be in concordance with the suggestion of Fry and colleagues of a strong functional association between the relatively simple venoms of sea snakes and their teleost-based diet of a single vertebrate class (fish) [80,81]. In contrast to some terrestrial elapid venoms that possess a complex protein pattern with a high number of isoforms, for example that of Micrurus nigrocinctus [82], the venom of P. platura might have evolved without a strong pressure for isoform diversification through gene duplication and divergence, or alternatively, might have undergone a secondary genetic simplification as part of its adaptation to the marine environment and a relatively specific type of prey, essentially consisting of small fish [24].…”

Section: Accepted M Manuscriptsupporting

confidence: 92%

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

View full text Add to dashboard Cite

Section: Accepted M Manuscriptsupporting

confidence: 92%

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

View full text Add to dashboard Cite

“…Mass spectrometry revealed a mixture of proteins (Fig. S1) as complex as that seen for snakes in similar analyses (12). Analysis of the mandibular venom gland cDNA library revealed a molecularly diverse transcriptome ( Table 1) with 35% of the 2000 transcripts encoding known toxin types from other Toxicofera venoms (6,9,13).…”

Section: Resultsmentioning

confidence: 64%

A central role for venom in predation by Varanus komodoensis (Komodo Dragon) and the extinct giant Varanus ( Megalania ) priscus

Fry

Wroe

Teeuwisse³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

129

130

View full text Add to dashboard Cite

The predatory ecology of Varanus komodoensis (Komodo Dragon) has been a subject of long-standing interest and considerable conjecture. Here, we investigate the roles and potential interplay between cranial mechanics, toxic bacteria, and venom. Our analyses point to the presence of a sophisticated combined-arsenal killing apparatus. We find that the lightweight skull is relatively poorly adapted to generate high bite forces but better adapted to resist high pulling loads. We reject the popular notion regarding toxic bacteria utilization. Instead, we demonstrate that the effects of deep wounds inflicted are potentiated through venom with toxic activities including anticoagulation and shock induction. Anatomical comparisons of V. komodoensis with V. (Megalania) priscus fossils suggest that the closely related extinct giant was the largest venomous animal to have ever lived. evolution ͉ phylogeny ͉ squamate ͉ protein ͉ toxin P redation by Varanus komodoensis, the world's largest extant lizard, has been an area of great controversy (cf. ref. 1). Three-dimensional finite element (FE) modeling has suggested that the skull and bite force of V. komodoensis are weak (2). However, the relevance of bite force and cranial mechanics to interpretations of feeding behavior cannot be fully evaluated in the absence of comparative data. Moreover, this previous analysis did not account for gape angle, which can significantly influence results (3). Irrespective of evidence for or against a powerful bite, V. komodoensis is clearly capable of opening wounds that can lead to death through blood loss (4). Controversially, the proposition that utilization of pathogenic bacteria facilitates the prey capture (4, 5) has been widely accepted despite a conspicuous lack of supporting evidence for a role in predation. In contrast, recent evidence has revealed that venom is a basal characteristic of the Toxicofera reptile clade (6), which includes the varanid lizards (7), suggesting a potential role of venom in prey capture by V. komodoensis that has remained unexplored. This is consistent with prey animals reported as being unusually quiet after being bitten and rapidly going into shock (4) and the anecdotal reports of persistent bleeding in human victims after bites (including B.G.F.'s personal observations). Shock-inducing and prolonged bleeding pathophysiological effects are also characteristic of helodermatid lizard envenomations (cf. ref . 8), consistent with the similarity between helodermatid and varanid venoms (6).Here, we examine the feeding ecology of V. komodoensis in detail. We compare the skull architecture and dentition with the related extinct giant V. priscus (Megalania). In this 3D finite element modeling of reptilian cranial mechanics that applies a comparative approach, we also compare the bite force and skull stress performance with that of Crocodylus porosus (Australian Saltwater Crocodile), including the identification of optimal gape angle (an aspect not considered in previous nonreptilian comparative FE analyses). We als...

show abstract

“…Despite this fascinating observation, the evolution and bioactivity of these atypical SVMP remain completely unexplored. Mass spectrometry of P. mossambicus venom revealed an abundance and diversity of peptides with molecular weights consistent to post-translational proteolytically liberated peptides from the propetide precursor region (22).…”

mentioning

confidence: 91%

Differential Evolution and Neofunctionalization of Snake Venom Metalloprotease Domains

Brust

Sunagar

Undheim

et al. 2013

Molecular & Cellular Proteomics

Self Cite

View full text Add to dashboard Cite

Snake venom metalloproteases (SVMP) are composed of five domains: signal peptide, propeptide, metalloprotease, disintegrin, and cysteine-rich. Secreted toxins are typically combinatorial variations of the latter three domains. The SVMP-encoding genes of Psammophis mossambicus venom are unique in containing only the signal and propeptide domains. We show that the Psammophis SVMP propeptide evolves rapidly and is subject to a high degree of positive selection. Unlike Psammophis, some species of Echis express both the typical multidomain and the unusual monodomain (propeptide only) SVMP, with the result that a lower level of variation is exerted upon the latter. We showed that most mutations in the multidomain Echis SVMP occurred in the protease domain responsible for proteolytic and hemorrhagic activities. The cysteinerich and disintegrin-like domains, which are putatively responsible for making the P-III SVMPs more potent than the P-I and P-II forms, accumulate the remaining variation. Thus, the binding sites on the molecule's surface are evolving rapidly whereas the core remains relatively conserved. Bioassays conducted on two post-translationally cleaved novel proline-rich peptides from the P. mossambicus propeptide domain showed them to have been neofunctionalized for specific inhibition of mammalian a7 neuronal nicotinic acetylcholine receptors. We show that the proline rich postsynaptic specific neurotoxic peptides from Azemiops feae are the result of convergent evolution within the precursor region of the C-type na- Snake venom metalloproteases (SVMP)1 evolved from ADAM (A disintegrin and metalloprotease) proteins that were recruited into the venom of snakes near the base of the advanced snake (Caenophidia) radiation. They have been identified in the venoms of all lineages of advanced snakes (1-5). The ancestral SVMP (P-III) contains (in downstream order) five domains: signal ϩ propeptide ϩ metalloprotease ϩ disintegrin ϩ cysteine rich. Following the divergence of vipers from the remaining caenophidians, extensive gene duplication, domain loss, and positive selection resulted in generation of the P-I and P-II classes of SVMP within the viperid lineage (6 -8). These two derived classes found in viper venoms lack either the cysteine-rich domain (P-II) or the cysteinerich and disintegrin domains (P-I) (8, 9). The signal peptide and the propeptide domain are typically cleaved off before expression although the latter has been detected in venoms on occasion (9). SVMP are often the dominant venom component in the venom of viperid snakes, but are typically much less significant in the venom of other snake families (10 -15). The majority of SVMP principally exhibit hemorrhagic activity, although other functions, such as the activation of prothrombin and Factor X, fibrin(ogen)olysis, apoptosis and the inhibition of platelet aggregation, have also been reported (16). Although SVMP-induced hemorrhage is primarily dependent on the proteolytic activity of the metalloprotease domain, the potency of this activity is incr...

show abstract

Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: evolutionary and toxinological implications

Cited by 153 publications

References 48 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

A central role for venom in predation by Varanus komodoensis (Komodo Dragon) and the extinct giant Varanus ( Megalania ) priscus

Differential Evolution and Neofunctionalization of Snake Venom Metalloprotease Domains

Contact Info

Product

Resources

About