Proteomic analysis to unravel the complex venom proteome of eastern India Naja naja: Correlation of venom composition with its biochemical and pharmacological properties

Dutta, Sumita; Chanda, Abhishek; Kalita, Bhargab; Islam, Taufikul; Patra, Aparup; Mukherjee, Ashis K.

doi:10.1016/j.jprot.2016.12.018

Cited by 101 publications

(65 citation statements)

References 94 publications

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“…Other elapids exhibit more complex venoms; even though they are often dominated by one or two venom protein superfamilies (typically 3FTxs and PLA 2 s), they have a greater number of individual protein isoforms within each of these families, with at least 12 3FTx isoforms, and usually more, present in venoms. This includes the diverse genera Micrurus, Naja, Ophiophagus, Dendroaspis and Bungarus [53][54][55][56][57][58]. Even the rear-fanged snake B. irregularis produces a venom with at least 25 different 3FTx isoforms, 10 of which are abundant [36].…”

Section: Discussionmentioning

confidence: 99%

Adaptive evolution of distinct prey-specific toxin genes in rear-fanged snake venom

et al. 2018

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Venom proteins evolve rapidly, and as a trophic adaptation are excellent models for predator-prey evolutionary studies. The key to a deeper understanding of venom evolution is an integrated approach, combining prey assays with analysis of venom gene expression and venom phenotype. Here, we use such an approach to study venom evolution in the Amazon puffing snake, , a generalist feeder. We identify two novel three-finger toxins: sulditoxin and sulmotoxin 1. These new toxins are not only two of the most abundant venom proteins, but are also functionally intriguing, displaying distinct prey-specific toxicities. Sulditoxin is highly toxic towards lizard prey, but is non-toxic towards mammalian prey, even at greater than 22-fold higher dosage. By contrast, sulmotoxin 1 exhibits the reverse trend. Furthermore, evolutionary analysis and structural modelling show highest sequence variability in the central loop of these proteins, probably driving taxon-specific toxicity. This is, to our knowledge, the first case in which a bimodal and contrasting pattern of toxicity has been shown for proteins in the venom of a single snake in relation to diet. Our study is an example of how toxin gene neofunctionalization can result in a venom system dominated by one protein superfamily and still exhibit flexibility in prey capture efficacy.

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Section: Discussionmentioning

confidence: 99%

Adaptive evolution of distinct prey-specific toxin genes in rear-fanged snake venom

et al. 2018

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“…Tandem mass spectrometry coupled to protein database search has evolved as a gold standard for snake venom protein identification 11 – 13 . Although, several isotope labeling methods such as SILAC, ICAT, and iTRAQ, are applied for mass spectrometry-based protein quantification 24 , albeit some limitations of these techniques may restrict their use for quantification of venom proteins 24 , 25 .…”

Section: Resultsmentioning

confidence: 99%

“…Although traditional methods (chromatographic separation of venom proteins followed by biochemical assays) have long been used to investigate snake venom composition 6 – 8 , they have been inadequate to unravel the detail composition of complex venom proteomes. In contrast, the modern proteomic approach has eliminated most shortcomings of classical chromatographic techniques when followed by biochemical assays to identify the venom proteins 9 – 13 . Although tandem mass spectrometry-based protein identification is limited because of the absence of sufficient sequences in the protein database repository, it can contribute to the quantitative identification of venom proteomes 14 .…”

Section: Introductionmentioning

confidence: 99%

Proteomics and antivenomics of Echis carinatus carinatus venom: Correlation with pharmacological properties and pathophysiology of envenomation

Patra

Kalita

Chanda

et al. 2017

Sci Rep

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140

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The proteome composition of Echis carinatus carinatus venom (ECV) from India was studied for the first time by tandem mass spectrometry analysis. A total of 90, 47, and 22 distinct enzymatic and non-enzymatic proteins belonging to 15, 10, and 6 snake venom protein families were identified in ECV by searching the ESI-LC-MS/MS data against non-redundant protein databases of Viperidae (taxid 8689), Echis (taxid 8699) and Echis carinatus (taxid 40353), respectively. However, analysis of MS/MS data against the Transcriptome Shotgun Assembly sequences (87 entries) of conger E. coloratus identified only 14 proteins in ECV. Snake venom metalloproteases and snaclecs, the most abundant enzymatic and non-enzymatic proteins, respectively in ECV account for defibrinogenation and the strong in vitro pro-coagulant activity. Further, glutaminyl cyclase, aspartic protease, aminopeptidase, phospholipase B, vascular endothelial growth factor, and nerve growth factor were reported for the first time in ECV. The proteome composition of ECV was well correlated with its biochemical and pharmacological properties and clinical manifestations observed in Echis envenomed patients. Neutralization of enzymes and pharmacological properties of ECV, and immuno-cross-reactivity studies unequivocally point to the poor recognition of <20 kDa ECV proteins, such as PLA2, subunits of snaclec, and disintegrin by commercial polyvalent antivenom.

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“…Thus there is convergence between the two groups in upright hooding displays being associated with defensive cytotoxic function, and as they have evolved the function independently the underlying chemical mechanisms are not homologous. Hemachatus + Naja venoms have a high concentration of the cytotoxic 3FTx unique to this clade [36,37,38,39,40,41,42,43,44,45]. Similarly O. hannah venoms have the highest concentration of L-amino acid oxidase of any snake venom and also the most derived forms of venom L-amino acid oxidase [23,46,47,48,49,50,51].…”

Section: Resultsmentioning

confidence: 99%

How the Cobra Got Its Flesh-Eating Venom: Cytotoxicity as a Defensive Innovation and Its Co-Evolution with Hooding, Aposematic Marking, and Spitting

Panagides

Jackson

Ikonomopoulou

et al. 2017

Toxins

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The cytotoxicity of the venom of 25 species of Old World elapid snake was tested and compared with the morphological and behavioural adaptations of hooding and spitting. We determined that, contrary to previous assumptions, the venoms of spitting species are not consistently more cytotoxic than those of closely related non-spitting species. While this correlation between spitting and non-spitting was found among African cobras, it was not present among Asian cobras. On the other hand, a consistent positive correlation was observed between cytotoxicity and utilisation of the defensive hooding display that cobras are famous for. Hooding and spitting are widely regarded as defensive adaptations, but it has hitherto been uncertain whether cytotoxicity serves a defensive purpose or is somehow useful in prey subjugation. The results of this study suggest that cytotoxicity evolved primarily as a defensive innovation and that it has co-evolved twice alongside hooding behavior: once in the Hemachatus + Naja and again independently in the king cobras (Ophiophagus). There was a significant increase of cytotoxicity in the Asian Naja linked to the evolution of bold aposematic hood markings, reinforcing the link between hooding and the evolution of defensive cytotoxic venoms. In parallel, lineages with increased cytotoxicity but lacking bold hood patterns evolved aposematic markers in the form of high contrast body banding. The results also indicate that, secondary to the evolution of venom rich in cytotoxins, spitting has evolved three times independently: once within the African Naja, once within the Asian Naja, and once in the Hemachatus genus. The evolution of cytotoxic venom thus appears to facilitate the evolution of defensive spitting behaviour. In contrast, a secondary loss of cytotoxicity and reduction of the hood occurred in the water cobra Naja annulata, which possesses streamlined neurotoxic venom similar to that of other aquatic elapid snakes (e.g., hydrophiine sea snakes). The results of this study make an important contribution to our growing understanding of the selection pressures shaping the evolution of snake venom and its constituent toxins. The data also aid in elucidating the relationship between these selection pressures and the medical impact of human snakebite in the developing world, as cytotoxic cobras cause considerable morbidity including loss-of-function injuries that result in economic and social burdens in the tropics of Asia and sub-Saharan Africa.

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Proteomic analysis to unravel the complex venom proteome of eastern India Naja naja: Correlation of venom composition with its biochemical and pharmacological properties

Cited by 101 publications

References 94 publications

Adaptive evolution of distinct prey-specific toxin genes in rear-fanged snake venom

Adaptive evolution of distinct prey-specific toxin genes in rear-fanged snake venom

Proteomics and antivenomics of Echis carinatus carinatus venom: Correlation with pharmacological properties and pathophysiology of envenomation

How the Cobra Got Its Flesh-Eating Venom: Cytotoxicity as a Defensive Innovation and Its Co-Evolution with Hooding, Aposematic Marking, and Spitting

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