Scientists Create Artificial Antibody to Defeat Lethal Snakebite Venom
Revolutionary breakthrough in snakebite treatment! Scientists unveil a synthetic antibody, a game-changer against deadly snake venom. Discover how this innovation offers universal protection, targeting cobras, kraits, and more. Say goodbye to traditional antivenom challenges!
Scientists have created a man-made antibody capable of neutralizing a lethal toxin produced by various snakes. The research, detailed in the journal Science Translational Medicine, utilized a method previously employed in screening for antibodies against HIV and COVID-19 to develop this new venom-neutralizing antibody.
Senji Laxme, a PhD student at the Indian Institute of Science (IISc), Bengaluru, emphasized that this marks the first application of this strategy in developing antibodies for snakebite treatment. The collaborative team, including researchers from the US-based Scripps Research Institute, views this study as a step toward a universal antibody solution offering broad protection against venom from different snakes, such as cobras, king cobras, kraits, and black mambas.
Snakebites cause numerous fatalities annually, particularly in India and sub-Saharan Africa. The current approach to antivenom development involves injecting snake venom into equines like horses, ponies, and mules, collecting antibodies from their blood. However, this method presents challenges, as these animals encounter various bacteria and viruses throughout their lives.
Kartik Sunagar, Associate Professor at IISc and joint corresponding author of the study, explained that antivenoms derived from this approach include antibodies against microorganisms, which are therapeutically unnecessary. Less than 10% of antivenom actually contains antibodies targeting snake venom toxins, as per research findings.
The recently created antibody homes in on a shared area at the heart of a potent toxin known as the three-finger toxin (3FTx), present in the venom of elapid snakes. While different elapid species produce varying 3FTxs, certain regions in the protein exhibit similarities. The researchers focused on one such conserved region – a disulphide core – and created a diverse library of artificial antibodies from humans, displayed on yeast cell surfaces.
Through rigorous screening, the team identified an antibody that strongly bound to various 3FTxs. Out of 149 3FTx variants in public repositories, this antibody successfully bound to 99. Subsequent tests in animal models, including mice injected with a toxic 3FTx from the Taiwanese banded krait, showed promising results. Mice given only the toxin succumbed within four hours, while those receiving the toxin-antibody mix survived past the 24-hour observation period and appeared completely healthy.
Similar positive outcomes were observed when testing the antibody against the venom of the monocled cobra from Eastern India and the black mamba from sub-Saharan Africa. The researchers concluded that the antibody’s efficacy was nearly 15 times greater than conventional products.
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