Proteomic analysis of Moroccan cobra Naja haje legionis venom using tandem mass spectrometry

Malih, Ibtissam; Rusmili, Muhamad Rusdi Ahmad; Tee, Ting Yee; Saı̈le, Rachid; Ghalim, Noreddine; Othman, Iekhsan

doi:10.1016/j.jprot.2013.11.012

Cited by 73 publications

(53 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Potent α-neurotoxicity preceded the evolution of the high-pressure front-fanged system of elapids, as was revealed by our discovery of α-colubritoxin, the first 3FTx isolated and characterized from a non-front-fanged lineage [59]. The toxin was of the same form as had been studied in elapid snakes previously, where they had been called ‘weak neurotoxins’ since they were only weakly potent on mice [137,138,139,140,141,142,143,144,145,146,147,148,149]. A problem that had also confounded studies of Boiga irregularis (brown tree snake), which had thus concluded they were non-venomous based on their effects in a murine model [150,151,152,153,154,155].…”

Section: Resultsmentioning

confidence: 99%

The Snake with the Scorpion’s Sting: Novel Three-Finger Toxin Sodium Channel Activators from the Venom of the Long-Glanded Blue Coral Snake (Calliophis bivirgatus)

Yang

Deuis

Dashevsky

et al. 2016

Toxins

View full text Add to dashboard Cite

Millions of years of evolution have fine-tuned the ability of venom peptides to rapidly incapacitate both prey and potential predators. Toxicofera reptiles are characterized by serous-secreting mandibular or maxillary glands with heightened levels of protein expression. These glands are the core anatomical components of the toxicoferan venom system, which exists in myriad points along an evolutionary continuum. Neofunctionalisation of toxins is facilitated by positive selection at functional hotspots on the ancestral protein and venom proteins have undergone dynamic diversification in helodermatid and varanid lizards as well as advanced snakes. A spectacular point on the venom system continuum is the long-glanded blue coral snake (Calliophis bivirgatus), a specialist feeder that preys on fast moving, venomous snakes which have both a high likelihood of prey escape but also represent significant danger to the predator itself. The maxillary venom glands of C. bivirgatus extend one quarter of the snake’s body length and nestle within the rib cavity. Despite the snake’s notoriety its venom has remained largely unstudied. Here we show that the venom uniquely produces spastic paralysis, in contrast to the flaccid paralysis typically produced by neurotoxic snake venoms. The toxin responsible, which we have called calliotoxin (δ-elapitoxin-Cb1a), is a three-finger toxin (3FTx). Calliotoxin shifts the voltage-dependence of NaV1.4 activation to more hyperpolarised potentials, inhibits inactivation, and produces large ramp currents, consistent with its profound effects on contractile force in an isolated skeletal muscle preparation. Voltage-gated sodium channels (NaV) are a particularly attractive pharmacological target as they are involved in almost all physiological processes including action potential generation and conduction. Accordingly, venom peptides that interfere with NaV function provide a key defensive and predatory advantage to a range of invertebrate venomous species including cone snails, scorpions, spiders, and anemones. Enhanced activation or delayed inactivation of sodium channels by toxins is associated with the extremely rapid onset of tetanic/excitatory paralysis in envenomed prey animals. A strong selection pressure exists for the evolution of such toxins where there is a high chance of prey escape. However, despite their prevalence in other venomous species, toxins causing delay of sodium channel inhibition have never previously been described in vertebrate venoms. Here we show that NaV modulators, convergent with those of invertebrates, have evolved in the venom of the long-glanded coral snake. Calliotoxin represents a functionally novel class of 3FTx and a structurally novel class of NaV toxins that will provide significant insights into the pharmacology and physiology of NaV. The toxin represents a remarkable case of functional convergence between invertebrate and vertebrate venom systems in response to similar selection pressures. These results underscore the dynamic evolution of the Toxicofera re...

show abstract

Section: Resultsmentioning

confidence: 99%

The Snake with the Scorpion’s Sting: Novel Three-Finger Toxin Sodium Channel Activators from the Venom of the Long-Glanded Blue Coral Snake (Calliophis bivirgatus)

Yang

Deuis

Dashevsky

et al. 2016

Toxins

View full text Add to dashboard Cite

show abstract

“…Shotgun-proteomics and LC–MS/MS approaches have been used to characterize many other snake venom proteomes, including kraits and cobras [17,18]. …”

Section: Resultsmentioning

confidence: 99%

Proteomic Characterization and Comparison of Malaysian Tropidolaemus wagleri and Cryptelytrops purpureomaculatus Venom Using Shotgun-Proteomics

Abidin

Rajadurai

Chowdhury

et al. 2016

Toxins

Self Cite

View full text Add to dashboard Cite

Tropidolaemus wagleri and Cryptelytrops purpureomaculatus are venomous pit viper species commonly found in Malaysia. Tandem mass spectrometry analysis of the crude venoms has detected different proteins in T. wagleri and C. purpureomaculatus. They were classified into 13 venom protein families consisting of enzymatic and nonenzymatic proteins. Enzymatic families detected in T. wagleri and C. purpureomaculatus venom were snake venom metalloproteinase, phospholipase A2, l-amino acid oxidase, serine proteases, 5′-nucleotidase, phosphodiesterase, and phospholipase B. In addition, glutaminyl cyclotransferase was detected in C. purpureomaculatus. C-type lectin-like proteins were common nonenzymatic components in both species. Waglerin was present and unique to T. wagleri—it was not in C. purpureomaculatus venom. In contrast, cysteine-rich secretory protein, bradykinin-potentiating peptide, and C-type natriuretic peptide were present in C. purpureomaculatus venom. Composition of the venom proteome of T. wagleri and C. purpureomaculatus provides useful information to guide production of effective antivenom and identification of proteins with potential therapeutic applications.

show abstract

“…Our knowledge on the proteomes of venom has advanced remarkably since then, shedding light on the improvement of snakebite management as well as drug discovery [26][27][28][29]. To date, the proteomes of a considerable number of medically important venomous snakes have been reported (for examples: [31][32][33][34][35][36]), however, there were limited studies published on the proteome of sea snake venoms [37][38].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…The findings of such a simplified venom proteome for H. schistosus is comparable to that reported for two other hydrophiid species: Hydrophis cyanocinctus with only 2 protein families [37] and Pelamis platura with 7 protein families [38], investigated using the similar methodology of reverse-phase HPLC, SDS-PAGE and peptide sequencing. Based on the proteomic findings, the toxin diversity of H. schistosus venom appears rather limited compared to some of its terrestrial elapidic relatives, such as cobras [31,32,34,36], king cobra [44] and kraits [33], which venom proteomes exhibit well beyond 30 proteins classified into at least 10 protein families. In addition, like many hydrophiids, the venom of H. schistosus is usually injected in a small concentrated amount yet capable of producing severe toxicity [14,21,37].…”

Section: Venom Proteome Of Hydrophis Schistosus: a Minimalist's Profilementioning

confidence: 99%

Venomics of the beaked sea snake, Hydrophis schistosus: A minimalist toxin arsenal and its cross-neutralization by heterologous antivenoms

Tan

Lim

et al. 2015

Journal of Proteomics

View full text Add to dashboard Cite

Proteomic analysis of Moroccan cobra Naja haje legionis venom using tandem mass spectrometry

Cited by 73 publications

References 36 publications

The Snake with the Scorpion’s Sting: Novel Three-Finger Toxin Sodium Channel Activators from the Venom of the Long-Glanded Blue Coral Snake (Calliophis bivirgatus)

The Snake with the Scorpion’s Sting: Novel Three-Finger Toxin Sodium Channel Activators from the Venom of the Long-Glanded Blue Coral Snake (Calliophis bivirgatus)

Proteomic Characterization and Comparison of Malaysian Tropidolaemus wagleri and Cryptelytrops purpureomaculatus Venom Using Shotgun-Proteomics

Venomics of the beaked sea snake, Hydrophis schistosus: A minimalist toxin arsenal and its cross-neutralization by heterologous antivenoms

Contact Info

Product

Resources

About