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Velvet Ant Venom May Yield Answers for Pain-Related Medical Research

The AHA! Team — Wed, 26 Feb 2025 06:26:40 +0000

Indiana University via Newswise – The Scarlet Velvet Ant, which is actually a type of wasp, has a venomous sting that is described as explosive and akin to “hot oil from the deep fryer spilling over your entire hand.” The study authors focused on how the venom interacts with nerve cells responsible for sensing pain. A new study by researchers at Indiana University Bloomington investigates why velvet ant stings are among the most excruciating in the animal kingdom, and offers a fascinating glimpse into the evolutionary arms race between predators and prey—while providing insights that may inform pain-related medical research. The Scarlet Velvet Ant, which is actually a type of wasp, has a venomous sting that is described as explosive and akin to “hot oil from the deep fryer spilling over your entire hand.” But while the sting is incredibly painful, it’s not particularly toxic, which suggests that its primary function is to act as a deterrent rather than to kill. The insect’s sting, along with its striking red-and-black coloration, serves as a warning to predators and an enduring reminder of its formidable defense mechanisms. The study, recently published in Current Biology, was authored by Lydia Borjon, Assistant Scientist in in the Tracey Lab at the Gill Institute for Neuroscience at IU, Luana Assis Ferreira, postdoctoral researcher in the Hohmann Lab at the Gill Institute, Jonathan Trinidad, Senior Scientist in the College of Arts and Science’s Department of Chemistry, Andrea Hohmann, Professor in the College’s Psychological and Brain Sciences department and Linda and Jack Gill Chair of Neuroscience, Sunčica Šašić (Human Biology B.S. ’24), and Dan Tracey, Professor in the College’s Biology department and Linda and Jack Gill Chair of Neuroscience. Velvet ants, including the Scarlet Velvet Ant, are commonly found in the southern and eastern United States. They thrive in dry, sandy environments, and are often seen scurrying on the ground in search of nectar or other insects to parasitize. To understand how their venom works, the IU scientists turned to common fruit flies, Drosophila melanogaster, a common model organism for studying biological processes. (IU Bloomington is the home of three resource centers utilized by fruit fly researchers worldwide.) The study authors focused on how the venom interacts with nerve cells responsible for sensing pain. These cells, called nociceptors, respond to potentially harmful stimuli like extreme heat or sharp pressure. In fruit fly larvae, a specific group of these pain-sensing neurons was found to react strongly to velvet ant venom, even at extremely diluted concentrations. The team identified a key venom ingredient—a peptide called Do6a—that activates these nociceptors. Peptides are short chains of amino acids, and this particular one, Do6a, triggers pain-sensing ion channels in insects. (Ion channels are specialized proteins embedded in the membranes of cells that allow ions—charged particles—to pass in and out of the cell.) This ion movement is crucial for various physiological processes, including nerve impulse transmission, muscle contraction, and maintaining the cell’s resting potential. Notably, the targeted ion channels known as Pickpocket/Balboa (Ppk/Bba) in fruit flies bear a striking resemblance to Acid-Sensing Ion Channels (ASICs) found in vertebrates, including mammals and humans, highlighting a fascinating evolutionary link in how different organisms process pain stimuli. The Evolutionary Edge “Our study findings suggest that velvet ants target the pain-sensing systems of evolutionarily distant animals, including vertebrates, like mammals and birds, and invertebrates, like other insects, but it does so through different mechanisms” said Lydia Borjon. “We expected the simplest solution, that the venom would act through related receptors in both insects and mice, but we were surprised to find that this was not the case.” In fruit flies, the Do6a peptide is highly specialized and potent, while in mammals, other components of the venom—less potent and more generalized peptides—trigger the pain response. “Not only is Do6a a very strong activator of insect pain-sensing neurons, it is also the most abundant peptide in the venom. This implies that the defense against other insects was an important factor in the evolution of the venom contents,” Borjon added. This led the researchers to test the venom’s effectiveness against another insect species. They observed how praying mantises responded to being stung. The mantises displayed clear avoidance behaviors, underscoring the venom’s role as a powerful deterrent in the insect world. “This research underscores the incredible precision of evolutionary adaptations,” said Tracey. “Velvet ants have refined their venom to exploit specific molecular targets in a way that maximizes their survival advantage. It is remarkable that the venom evolved to target the nociception systems of vertebrates and invertebrates with such precision.” Species-specific adaptations and implications for pain research The researchers used advanced imaging techniques to observe how nerve cells in fruit fly larvae reacted to venom. They also conducted genetic experiments to confirm the role of Ppk/Bba ion channels. When these channels were removed or deactivated, the nerve cells stopped responding to the venom, proving that the channels are essential for the venom’s effects. When it came to vertebrates, the researchers tested the venom on mice. They found that certain peptides in the venom caused the mice to exhibit pain-related behaviors, such as licking, flinching or shaking the injected paw. However, the Do6a peptide, which was so potent in insects, had no noticeable effect on the mice, highlighting the venom’s species-specific adaptations. ”Exploring how velvet ant venom affects different species provides valuable insights into pain pathways, with potential implications for advancing medical research” said Luana de Assis Ferreira. “For instance, the study highlights how specific ion channels are involved in triggering pain. Such knowledge might one day help scientists develop new painkillers or treatments for chronic pain by targeting similar pathways in humans.” While velvet ant’s venom is a marvel of evolutionary engineering, the broader implications are equally compelling. “This study provides a framework for exploring how other animal venoms work, especially those that target pain pathways. Venoms are a treasure trove of bioactive compounds, and studying them often leads to breakthroughs in pharmacology and medicine”, said Andrea Hohmann. “This research offers a deeper appreciation of nature’s complexity and the power of natural selection, in that the velvet ant’s sting is a carefully honed defense mechanism that ensures its survival in a dangerous world filled with potential predators, said Tracey. “And with these findings, we’re one step closer to understanding, and maybe even harnessing, its power.” To read the original article click here.

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New Antidote for Cobra Bites Discovered

The AHA! Team — Wed, 31 Jul 2024 08:28:41 +0000

University of Sydney via EurekAlert! – Cheap, available drug could help reduce impact of snakebites worldwide Scientists at the University of Sydney and Liverpool School of Tropical Medicine have made a remarkable discovery: a commonly used blood thinner, heparin, can be repurposed as an inexpensive antidote for cobra venom. Cobras kill thousands of people a year worldwide and perhaps a hundred thousand more are seriously maimed by necrosis – the death of body tissue and cells – caused by the venom, which can lead to amputation. Cobras kill thousands of people a year worldwide Current antivenom treatment is expensive and does not effectively treat the necrosis of the flesh where the bite occurs. “Our discovery could drastically reduce the terrible injuries from necrosis caused by cobra bites – and it might also slow the venom, which could improve survival rates,” said Professor Greg Neely, a corresponding author of the study from the Charles Perkins Centre and Faculty of Science at the University of Sydney. Using CRISPR gene-editing technology to identify ways to block cobra venom, the team, which consisted of scientists based in Australia, Canada, Costa Rica and the UK, successfully repurposed heparin (a common blood thinner) and related drugs and showed they can stop the necrosis caused by cobra bites. The research is published today on the front cover of Science Translational Medicine. PhD student and lead author, Tian Du, also from the University of Sydney, said: “Heparin is inexpensive, ubiquitous and a World Health Organization-listed Essential Medicine. After successful human trials, it could be rolled out relatively quickly to become a cheap, safe and effective drug for treating cobra bites.” The team used CRISPR to find the human genes that cobra venom needs to cause necrosis that kills the flesh around the bite. One of the required venom targets are enzymes needed to produce the related molecules heparan and heparin, which many human and animal cells produce. Heparan is on the cell surface and heparin is released during an immune response. Their similar structure means the venom can bind to both. The team used this knowledge to make an antidote that can stop necrosis in human cells and mice. The heparinoid drugs act as a ‘decoy’ antidote Unlike current antivenoms for cobra bites, which are 19th century technologies, the heparinoid drugs act as a ‘decoy’ antidote. By flooding the bite site with ‘decoy’ heparin sulfate or related heparinoid molecules, the antidote can bind to and neutralize the toxins within the venom that cause tissue damage. Joint corresponding author, Professor Nicholas Casewell, Head of the Centre for Snakebite Research & Interventions at Liverpool School of Tropical Medicine, said: “Snakebites remain the deadliest of the neglected tropical diseases, with its burden landing overwhelmingly on rural communities in low- and middle-income countries. “Our findings are exciting because current antivenoms are largely ineffective against severe local envenoming, which involves painful progressive swelling, blistering and/or tissue necrosis around the bite site. This can lead to loss of limb function, amputation and lifelong disability.” Snakebites kill up to 138,000 people a year, with 400,000 more experiencing long-term consequences of the bite. While the number affected by cobras is unclear, in some parts of India and Africa, cobra species account for most snakebite incidents. Snakebites kill up to 138,000 people a year The World Health Organization has identified snakebite as a priority in its program for tackling neglected tropical diseases. It has announced an ambitious goal of reducing the global burden of snakebite in half by 2030. Professor Neely said: “That target is just five years away now. We hope that the new cobra antidote we found can assist in the global fight to reduce death and injury from snakebite in some of the world’s poorest communities.” Working in the Dr John and Anne Chong Laboratory for Functional Genomics at the Charles Perkins Centre, Professor Neely’s team takes a systematic approach to finding drugs to treat deadly or painful venoms. It does this using CRISPR to identify the genetic targets used by a venom or toxin inside humans and other mammals. It then uses this knowledge to design ways to block this interaction and ideally protect people from the deadly actions of these venoms. This approach was used to identify an antidote to box jellyfish venom by the team in 2019. Professor Casewell leads the Centre for Snakebite Research & Interventions at the Liverpool School of Tropical Medicine (LSTM). The centre has conducted a diverse portfolio of research activities to better understand the biology of snake venoms and improve the efficacy, safety and affordability of antivenom treatment for tropical snakebite victims for more than 50 years. It boasts some of the world’s leading snakebite experts and has access to LSTM’s herpetarium, the largest and most diverse collection of tropical venomous snakes in the UK. RESEARCH Du, T. et al, ‘Molecular dissection of cobra venom highlights heparinoids as an effective snakebite antidote’. (Science Translational Medicine, 2024) DOI: 10.1126/scitranslmed.adk4802 JOURNAL Science Translational Medicine ARTICLE TITLE Molecular dissection of cobra venom highlights heparinoids as an effective snakebite antidote ARTICLE PUBLICATION DATE 17-Jul-2024 To read the original article click here.

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