Researchers have made a breakthrough in snakebite treatment using artificial intelligence to design two proteins that neutralize deadly venom toxins. These 'de novo' proteins, not found in nature, protected mice from fatal envenomation in lab experiments. This approach could lead to cheaper, safer, and more effective remedies than traditional antivenoms.
Each year, snake bites kill upwards of 100,000 people and permanently disable hundreds of thousands more, according to estimates from the World Health Organization. Promising new science, enabled by state-of-the-art technology, could help quell the threat. Researchers have successfully designed two proteins to neutralize some of the most lethal venom toxins, using a suite of artificial intelligence tools, per a study published January 15 in the journal Nature.
These “de novo” proteins–molecules not found anywhere in nature–protected 100% of mice from certain death when mixed with the deadly snake compounds and administered in lab experiments. “I think we could revolutionize the treatment,” says Susana Vázquez Torres, lead study author and a biochemist who completed this research as part of her doctoral thesis in David Baker’s lab at the University of Washington. Baker won the 2024 Nobel Prize in Chemistry for his work creating new proteins. This week’s publication is a continuation of that line of inquiry. “This study, of course, doesn’t solve the whole problem, but it demonstrates that we can develop molecules super quickly compared to traditional methods–and it works,” Vázquez Torres tells Popular Science. The strategy could lead to cheaper, safer, and more effective remedies than the status quo, she adds. “It’s fantastic work,” says Joseph Jardine, an assistant professor of immunology and microbiology at the Scripps Research Institute. Jardine wasn’t involved in the new study, but has previously published research developing synthetic antivenoms for the same sorts of compounds. This new research is both a demonstration of how far protein design has come in recent years, enabled by rapidly improving AI, and also an exciting practical advance in medicine, he says.Despite the toll that snake bites take, the treatment for envenomings has been the same for more than a century: Antibodies collected from horses or other animals inoculated with sub-lethal amounts of venom. These antivenoms save lives, but they have some serious downsides. For one, they’re expensive and difficult to make as producing them involves maintaining stables of animals. Plus, they vary in quality as relying on imperfect immune systems yields uneven results, and antivenoms tend to work better against some toxins than others–only partially neutralizing the smallest components of the complex cocktail that is venom, and performing poorly against some species’ bites. They can trigger allergic reactions and other adverse side effects in recipients. And, because they’re a biological product, traditional antivenoms are very sensitive to temperature and need to be refrigerated for storage and transport–adding to the cost and inaccessibility. In rural areas of Global South countries where snake bites are especially common, the treatment is particularly difficult to get. In contrast, the newly designed proteins are stable across a much wider range of temperatures, can potentially be produced in bulk using microorganisms like yeast, may prompt fewer side effects, and would be easier to fine tune and keep consistent. “These small de novo proteins have a number of really interesting advantages, including thermal stability, the cost of manufacturing, and the fact that they can target something in a way that an antibody might not be able to,” Jardine explains. One day, such a product might be deliverable in an “EpiPen-like device,” readily available out in the field where it’s most needed, he suggests. Snake venoms are made up of many different toxins mixed together. Vázquez Torres and her colleagues focused their work on three-finger toxins (3FTx), deadly compounds that traditional antivenoms often perform poorly against. 3FTxs are especially prominent in the venom of elapids, the family of snakes which includes cobras, mambas, and coral snakes. These toxins (proteins themselves) wreak havoc in the mammalian body. Some are paralyzing neurotoxins, others destroy cells and damage tissue. The scientists sought to identify antidote proteins to combat three representative target toxins: a short-chain alpha neurotoxin, a long-chain alpha neurotoxin, and a cytotoxin. All three representative toxins are well studied, and so the scientists knew their intricate shapes from the start. From that base, they could identify the key binding sites they’d need to block to render each toxin inactive. They fed this information into the first of their AI tools called RoseTTAFold diffusion, a model similar to image generators like Dall-E and Midjourney, but one trained and specialized to output mock-ups of protein structures in accordance with requested criteria. In this case, the criteria were the toxin structures and the selected binding “hot spots,” that the researchers were hoping to clog u
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