Russell’s Viper – Hemotoxic Venom | Details – Types, Effects, and Pharmacology

Russel’s Viper is highly venomous and possesses hemotoxic venom (RVV – Russel’s Viper Venom) which is highly lethal. A small jab with the fangs can transfer a large amount of venom, which can cause coagulopathies, internal bleeding, tissue damage (necrosis), and acute kidney injury.

Russel’s Viper (Daboia russelii) is a hemotoxic venomous snake. It is one of the snakes in the Big 4 category (Russel’s Viper, Common Krait, Indian Cobra, and Indian Saw-scaled Viper). It was named after Patrick Russel, a Scottish surgeon and herpetologist who worked in India.

Physical Structure

A robust snake with a moderately big body, the Russell’s viper normally grows to a length of 90–150 cm. It has a skull that is distinctively trapezoidal and has big, movable fangs. Its colouring might vary, but it often has a background colour of yellow or brown with a number of black, asymmetrical crossbands on its back.

Mode of living and movement

They are preferably nocturnal but not a general behaviour. They are generally slow-moving but during aggression, they can move very fast and inject venom using their large fangs with a single jab. They have got the nickname of 360o attackers because of their fast-moving aggression and attack.

They usually consume small mammals, rodents, birds, etc. They use their hemotoxic venom to immobilize their prey. Their presence is found in grasslands, agricultural lands, coastal lowlands and bushy areas.

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Venom

Russel’s Viper is highly venomous and possesses hemotoxic venom (RVV – Russel’s Viper Venom) which is highly lethal. A small jab with the fangs can transfer a large amount of venom, which can cause coagulopathies, internal bleeding, tissue damage (necrosis), and acute kidney injury.

Snake venoms including RVV are highly proteinaceous. It involves toxins like metalloproteinases, phospholipase A2, and serine proteases. These toxic proteins can cause the above-mentioned body malfunctions.

The 70% venom of Russel’s Viper is stored in the fangs. During biting almost 70% of the stored venom is emptied as it can cause severe envenomation. This type of venom is a procoagulant. This has the ability to activate the serine endopeptidase (Factor X), which mediates the coagulation system. Subsequently, swelling and pain will occur at the site of the bite.

RVV Factor X Activator (RVV-X) is a metalloprotein that can activate the clotting system of the blood (Factor X), which activates the rapid floating of the victim/prey’s blood leading to death. RVV-V or Russel’s Viper Venom Factor V Activator is a glycoprotein variant. RVV-V can contain 12 cystines as well as 6 disulfide bonds.

Russell's viper venom serine proteinase, RVV-V (closed-form)
Figure: Russell’s viper venom serine proteinase, RVV-V (closed-form); Image: RCSB PDB

Pharmacology

RVV has the ability to activate blood clotting due to the RVV-X. That means it can induce a biological process called thrombosis. This is used as a principle for the dRVVT test or dilute Russel’s Viper Venom Time test. The RVV directly activates Factor X which leads to fibrin clots by turning prothrombin into thrombin. The prolonged and short duration of the clot depends upon the amount of phospholipids. This can be used for the analysis of the dRVVT test. (More Clinical and Research confirmations/statements are required. To be updated later)

References

  1. Juliana Castro-Amorim, Ana Oliveira, Ashis K. Mukherjee, Maria J. Ramos, and Pedro A. FernandesJournal of Chemical Information and Modeling 2023 63 (13), 4056-4069DOI: 10.1021/acs.jcim.2c01156
  2. Bawaskar, Himmatrao S., and Pramodini H. Bawaskar. “Diagnosis of Envenomation by Russell’s and Echis Carinatus Viper: A Clinical Study at Rural Maharashtra State of India.” Journal of Family Medicine and Primary Care, vol. 8, no. 4, 2019, pp. 1386-1390, https://doi.org/10.4103/jfmpc.jfmpc_156_19. Accessed 08 Oct. 2023.
  3. Castro-Amorim, Juliana et al. “Unraveling the Reaction Mechanism of Russell’s Viper Venom Factor X Activator: A Paradigm for the Reactivity of Zinc Metalloproteinases?.” Journal of chemical information and modeling vol. 63,13 (2023): 4056-4069. doi:10.1021/acs.jcim.2c01156
  4. Rand, Jacob H., and Lucia R. Wolgast. “Antiphospholipid Syndrome: Pathogenesis, Clinical Presentation, Diagnosis, and Patient Management.” Consultative Hemostasis and Thrombosis (Third Edition), 2012, pp. 324-341, https://doi.org/10.1016/B978-1-4557-2296-9.00020-8. Accessed 09 Oct. 2023.
  5. Wolgast, Lucia R. “Laboratory Diagnosis of Lupus Anticoagulant and Antiphospholipid Antibodies.” Transfusion Medicine and Hemostasis (Third Edition), 2018, pp. 925-931, https://doi.org/10.1016/B978-0-12-813726-0.00158-6. Accessed 09 Oct. 2023.

Author: Achuth B S | Edited by: Neethu Krishna

Published & Updated

Graduated from the University of Kerala with B.Sc. Botany and Biotechnology. M.Sc. Biotechnology from the University of Kerala. Attended certificate course in Artificial Intelligence for Everyone from Deeplearning.AI, Influenza Prevention and Control from World Health Organization. Attended workshops related to Bioinformatics at the University of Kerala. 3 years of experience in website management. Experience in WordPress, Blogger, Google Analytics, and Google Search Console.

Achuth B S

Graduated from the University of Kerala with B.Sc. Botany and Biotechnology. M.Sc. Biotechnology from the University of Kerala. Attended certificate course in Artificial Intelligence for Everyone from Deeplearning.AI, Influenza Prevention and Control from World Health Organization. Attended workshops related to Bioinformatics at the University of Kerala. 3 years of experience in website management. Experience in WordPress, Blogger, Google Analytics, and Google Search Console.

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