Dataset Information

Explaining Echis envenoming: Transcriptomic and proteomic profiling of Echis carinatus venom

ABSTRACT: In India, venom research has largely focussed on the ‘big four’ snakes that are greatly responsible for the burden of snakebite in the Indian subcontinent. This study aims to advance understanding of saw-scaled viper venoms from India, we implemented a multi-faceted approach. We sequenced the venom gland transcriptome of E. carinatus for the first time, while also characterising its venom proteome. This was followed by the evaluation of the biochemical activities of the major toxins in E. carinatus venoms. Finally, we assessed the in vitro binding efficacy and in vivo neutralising potency of commercial antivenoms against E. carinatus

INSTRUMENT(S):

ORGANISM(S): Echis Carinatus

TISSUE(S): Venom Gland

SUBMITTER: Kartik Sunagar

LAB HEAD: Kartik Sunagar

PROVIDER: PXD064002 | Pride | 2025-08-04

REPOSITORIES: Pride

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Explaining Echis: Proteotranscriptomic Profiling of Echis carinatus carinatus Venom.

Javed Salil S Gond Prasad Gopalkrishna PG Samanta Arpan A Unawane Ajinkya A Mudavath Muralidhar Nayak MN Jaglan Anurag A Sunagar Kartik K

Toxins 20250716 7

Snakebite remains the most neglected tropical disease globally, with India experiencing the highest rates of mortality and morbidity. While most envenomation cases in India are attributed to the 'big four' snakes, research has predominantly focused on Russell's viper (Daboia russelii), spectacled cobra (Naja naja), and common krait (Bungarus caeruleus), leading to a considerable gap in our understanding of saw-scaled viper (Echis carinatus carinatus) ven ...[more]

PMID: 40711164

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Project description:Assassin bugs (Hemiptera: Heteroptera: Reduviidae) are venomous insects that prey on invertebrates. Assassin bug venom has features in common with venoms from other animals, such as paralysing and lethal activity when injected, and a molecular composition that includes disulfide-rich peptide neurotoxins. Uniquely, this venom also has strong liquefying activity that has been hypothesised to facilitate feeding through the narrow channel of the proboscis—a structure inherited from sap- and phloem-feeding phytophagous hemipterans and adapted during the evolution of Heteroptera into a fang and feeding structure. However, further understanding of the function of assassin bug venom is impeded by the lack of proteomic studies detailing its molecular composition. In addition, the lack of knowledge regarding venoms of predaceous reduviids limits our understanding of how the venoms of the blood-feeding kissing bugs (Reduviidae: Triatominae) evolved to facilitate hematophagy. By using a combined transcriptomic/proteomic approach we show that the venom proteome of the harpactorine assassin bug Pristhesancus plagipennis includes a complex suite of >100 proteins comprising disulfide-rich peptides, CUB-domain proteins, cystatins, putative cytolytic toxins, triabin-like protein, odorant binding protein, serine proteases, catabolic enzymes, putative nutrient-binding proteins, plus eight families of proteins without homology to characterised proteins. Serine proteases, CUB domain proteins and other novel proteins in the 10–16 kDa mass range, as well as putative cytolytic toxins, were the most abundant venom components. Thus, in addition to putative neurotoxins, assassin bug venom includes a high proportion of enzymatic and cytolytic venom components well suited to tissue liquefaction. While some protein families such as lipocalin/triabins occur in the venoms of both predaceous and blood-feeding reduviids, the composition of venoms in these two groups differs markedly. These results provide insights into the venom evolution in the insect suborder Heteroptera.

Project description:Background The phenotypic polymorphism in rattlesnake venoms has been thoroughly documented, showing a dichotomy between haemorrhagic (Type I) and neurotoxic (Type II) venoms. In South America, the Type II phenotype is predominant; however, evidence exists of Type I haemorrhagic venoms in C. d. ruruima, raising questions about the efficacy of the Crotalus antivenom prepared for the Type II phenotype in treating Crotalus Type I snakebite patients, for whom the administration of Bothrops-Crotalus antivenom has been proposed. Methodology/Principal Findings This study characterises the dichotomy of C. d. ruruima venom based on the structure of isoforms differentially expressed in Type I and Type II venoms, the biological activities of each phenotype, and the implications for the clinical management of snakebites in Northern Brazil. Four toxins were differentially expressed in Type I and Type II venoms: two PIII-class SVMPs, which were highly expressed in Type I venoms and associated with proteolytic and haemorrhagic activity, and two PLA2s, corresponding to Crotoxin A and B chains, identified in Type II venoms and associated with increased phospholipase A2, myotoxic activities, and heightened lethality. The structure of Crotoxin chains was well conserved compared to C. d. terrificus crotoxin. However, compared to Bothropasin, the SVMP sequences exhibited several substitutions in functional and immunoreactive regions, resulting in low haemorrhagic activity and slight reactivity/neutralisation by Bothrops antivenom. In opposition, Crotalus antivenom reacted with high antibody titres and neutralised all activities of both venom subtypes, except the low haemorrhagic activity induced by Type I venoms. Conclusions/Significance The efficacy of Bothrops antivenom in incidents involving snakes of the Type I phenotype remains uncertain, and we advocate for an urgent prospective study in Roraima to assess the outcomes and benefits for patients receiving either Bothrops-Crotalus or solely Crotalus antivenoms following rattlesnake bites. Meanwhile, administering Bothrops-Crotalus antivenom could be warranted. However, it is crucial to remain aware of the issues of injecting heterologous Bothrops antibodies with limited efficacy in treating Crotalus snakebite patients.

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	EcCaKA08_F11.raw	Raw
	EcCaKA08_F12a.raw	Raw

Dataset Information

Explaining Echis envenoming: Transcriptomic and proteomic profiling of Echis carinatus venom

Dataset's files

Publications

Explaining <i>Echis</i>: Proteotranscriptomic Profiling of <i>Echis carinatus carinatus</i> Venom.

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Dataset Information

Explaining Echis envenoming: Transcriptomic and proteomic profiling of Echis carinatus venom

Dataset's files

Publications

Explaining &lt;i&gt;Echis&lt;/i&gt;: Proteotranscriptomic Profiling of &lt;i&gt;Echis carinatus carinatus&lt;/i&gt; Venom.

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OmicsDI is part of the ELIXIR infrastructure

Tweets

Explaining <i>Echis</i>: Proteotranscriptomic Profiling of <i>Echis carinatus carinatus</i> Venom.