July 7, 2025

Reducing Snakebite Mortality: Advances in Venom Research

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A new study has uncoded the mysteries of how the venom of Pope’s pit viper, a snake species native to northern and northeastern parts of India, works. The study can help establish the foundation for venom toxicity, pharmaceutical advancements, and enhanced antivenom compositions.

The “Big Four” venomous snakes—Russell’s Viper, Saw-Scaled Viper, Spectacled Cobra, and Common Krait—have undergone considerable research, but venom composition of Pope’s Pit Viper (Trimeresurus popeiorum) an arboreal, nocturnal serpent indigenous to the dense forests of Northeast India, remains unexamined.

Prof. Ashis K. Mukherjee, Director of the Institute of Advanced Study in Science and Technology, an autonomous institution of the Department of Science and Technology (DST) spearheaded a recent investigation along with Prof. B.G. Nair, Dr. M. Vanuopadath, Dr. Bhargab Kalita, and Dr. Aparup Patra from Amrita Vishwa Vidyapeetham, as well as Dr. H.T. Lalremsanga from Mizoram University, to elucidate the venom composition of this elusive pit viper.

Contemporary label-free quantitative proteomics identified 106 proteins in the venom of Pope’s Pit Viper, categorized into 12 toxin families. Notably, 60% of its venom comprises enzymes that break down proteins and damage tissue, interfere with blood coagulation, and induce local haemorrhage.

This study explores the venom’s harmful components, which are mostly toxic enzymes and demonstrating their deleterious effects on the victim. For example, snake Venom metalloproteinases (SVMPs), a toxic enzyme of the Viperidae family of snakes including Pope’s Pit Viper, are demonstrated for causing bleeding, tissue breakdown, and blood clotting issues in victims.

The venom also contains enzymes called Serine Proteases (SVSPs), which hinder blood coagulation, a toxic enzyme phospholipases A2 which induce muscle injury and inflammation and, a non-enzymatic toxin Snaclecs (Snake C-type lectins) which affect blood platelet function and blood coagulation.

The absence of species-specific antivenoms complicates the treatment of snakebites in India. Commercial antivenoms counteract the venom of the ‘Big Four’ species, hence leaving patients bitten by pit vipers vulnerable to repercussions. This study underscores the necessity for broad-spectrum or region-specific antivenoms to counteract T. popeiorum venom.

By comprehending the proteomic complexity of Pope’s Pit Viper venom, researchers have established a foundation for venom toxicity, pharmaceutical advancements, and enhanced antivenom compositions.

As India endeavours to decrease snakebite mortality by 50% by 2030, such innovative research would facilitate transforming venom studies into life-saving medical treatments. This study was recently published in International Journal of Biological Macromolecules.

Daily News Bulletin

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