Tag Archives: venom

This Unusual Underwater “Blue Dragon” Battles Stolen Jellyfish Venom

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Far from the shore, in the immense stretches of the open ocean, resides an uncommon assembly of creatures known as “Neustons.”

This environment is a vast, two-dimensional layer of the ocean that bridges the atmosphere with the sea.

Among this group, one of the most fascinating beings is the blue dragon, a kind of sea slug, or naujibrance, more widely recognized as the blue dragon, the sea swallow, or Glaucus atlanticus.

Blue dragons float on the surface, buoyed by the air bubbles they have ingested. To evade predators, they employ a unique biological strategy called countershading.

The underside of their body, positioned upside down, exhibits a bright blue hue that camouflages it against the ocean below, concealing it from aerial hunters above.

Conversely, the side that hangs from the surface boasts silver stripes that mimic the shimmering ocean surface, aiding swimming predators in their upward gaze.

Overall, the blue dragon appears peculiar owing to its sea slug nature. The main body, measuring about 3cm (0.4 inches), seems somewhat sluggish, but it features elongated appendages resembling fingers of varying lengths.

These appendages are not used for waving or swimming; they are anatomical structures called ceratha, essentially serving as a secondary gill by extending the intestines and respiratory system to facilitate breathing.

Like many sea slug species, the Blue Dragon utilizes its ceratha as a weapon. They are notorious hunters, primarily targeting other blue-hued Neustons, including Portuguese man o’ war (Physalia physalis) and jellyfish-like creatures like blue buttons (Porpita porpita) and by-the-wind sailors (Velella velella).

Blue dragons can inject venom into these organisms without fear of being stung.

‘They are vicious hunters, and their main prey is the other members of Neuston’ – Photo credit: Matty Smith Photo

Remarkably, these sea slugs can recycle their prey’s toxins, maintaining them intact and incorporating them into their ceratha.

When threatened by predators, they can launch these toxins as a potent defense mechanism.

Modern challenges pose threats to Blue Dragons and their fellow Neuston inhabitants. A study conducted between Hawaii and California reveals that they inhabit the same remote regions of the infamous Pacific Ocean, including the Great Pacific Garbage Patch, where floating plastic debris accumulates due to swirling ocean currents.

One approach to combat this plastic pollution involves placing a net between two vessels to retrieve debris from the surface. However, this method could inadvertently capture a significant number of Neustons.

The complete ecological consequences of this method remain unclear, but it may have significant repercussions on the marine food web. These creatures serve as crucial food sources for a variety of marine species, such as sea turtles and seabirds.

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Source: www.sciencefocus.com

AI Uncovers 386 Potential Antibiotics in Animal Venom

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University of Pennsylvania researchers used a deep learning tool named Apex to explore a worldwide venom dataset in search of new antibiotic candidates.

Guan et al. Vococcus is a rich source of previously hidden antibiotic scaffolds, showing that merging experimental validation with extensive computational mining can enhance the search for urgently needed antibiotics. Image credits: Guan et al., doi: 10.1038/s41467-025-60051-6.

The increasing prevalence of antibiotic-resistant pathogens, especially Gram-negative bacteria, underscores the critical demand for new treatments.

Venococcus represents a vast, largely untapped source of bioactive molecules with potential antibacterial properties.

In their recent study, researcher César de La Fuente and his team analyzed a comprehensive database containing 16,123 poison proteins and over 40 million poison-encoded peptides via a vertex deep learning model.

The algorithm successfully pinpointed 386 candidate peptides that differ in structure and function from known antimicrobial peptides.

“These poisons are evolutionary wonders, yet their antibacterial capabilities have not been thoroughly examined,” said Dr. de la Fuente.

“Apex can rapidly explore extensive chemical landscapes, identifying exceptional peptides that combat some of the most stubborn pathogens worldwide.”

From the potential candidates selected by AI, scientists synthesized 58 peptide variants for laboratory assessment.

Remarkably, 53 of these demonstrated efficacy against drug-resistant bacteria such as E. coli and Staphylococcus aureus, at doses safe for human red blood cells.

“By combining computational analysis with traditional laboratory techniques, we achieved one of the most thorough antibiotic studies to date,” noted Dr. Marcelo Torres, co-author of the research.

“The platform has mapped over 2,000 novel antibacterial motifs, enhancing its capacity to eliminate or suppress bacterial growth through short, specific amino acid sequences within proteins or peptides.”

“Our team is now advancing the top peptide candidates towards the development of new antibiotics, optimizing them through medicinal chemistry modulation.”

results will be published in the journal Nature Communications.

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C. Guan et al. 2025. A global assessment of venom data for antibacterial discovery using artificial intelligence techniques. Nat Commun 16, 6446; doi:10.1038/s41467-025-60051-6

Source: www.sci.news

Decoding the Mystery Behind the Velvet Ant’s Venom and its Painful Sting

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Velvet ants inject venom through their abdomen and sting.

JoJo Dexter/Getty Images

The bite of a female velvet ant is one of the most painful in the animal kingdom. Now, researchers have shown that the venoms of these insects contain multiple proteins that make them highly effective against a wide range of victims, including invertebrates, mammals, birds, reptiles, and amphibians. I discovered it.

Velvet ants are actually members of the wingless wasp family, of which there are over 7,000 species. Justin Schmidt, the researcher who created the Schmidt Sting Index, described the pain of a sting as “explosive and long-lasting, making you scream and feel like you’re going crazy. Hot oil from a deep fryer spills all over your hand.” .”

When I looked into what was causing so much pain, Dan Tracy Researchers at Indiana University urged the public to carefully collect female scarlet velvet ants.Dasimtyla occidentalis) from the Indiana and Kentucky sites.

They tested fruit fly venom (Drosophila melanogaster),mouse(Mus musculus) and praying mantis (tenodera sinensis), potential predators of velvet ants.

One of the peptides the research team isolated from the venom, Do6a, clearly caused a response in the insects, but surprisingly not in the mice.

“That means the venom has evolved to include components that specifically target pain-sensing neurons in insects, and other components that target mammals,” Tracy says.

The researchers further tested this by having praying mantises attempt to capture velvet ants.

“We found that velvet ants are constantly stinging praying mantises in self-defense to escape their clutches,” Tracy says.

However, when tested with other peptides isolated from velvet ant venom, called Do10a and Do13a, the mice showed a strong pain response.

After discovering the peptide that activated neurons, the researchers compared the venom peptide sequences of four other species of velvet ants.

“They all have nearly the same version of the peptide that strongly activates the insect’s pain-sensing neurons.” Lydia Boljonteam members at Indiana University. “There are also some peptides that are similar to common neuron activators, but with some differences. Therefore, pain may be triggered in a similar way in other velvet ant species.”

This research could help develop new pain treatments for humans, Borjon said.

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Source: www.newscientist.com

Scientists unravel the composition of the unique toxin found in black widow spider venom

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Black widow spider venom contains a cocktail of seven specific latrotoxins, but only one, alpha-latrotoxin, targets vertebrates, including humans. chemist of University of Munster They have now deciphered the structure of alpha-latrotoxin before and after membrane insertion at near atomic resolution.

Cryo-EM structures of α-latrotoxin in two different tetrameric states. Image credit: Klink others., doi: 10.1038/s41467-024-52635-5.

Latrotoxin is the main toxic component of the venom of black widow spiders (genus). latrodectus).

The toxins include five insecticidal toxins known as α-latrotoxin, α-, β-, γ-, δ-, and ε-latroinsect toxins, which are unique to vertebrates, and one toxin that is unique to crustaceans.

“Alpha-latrotoxin interferes with nervous system signal transmission,” said researcher Björn Klinck and colleagues at the University of Münster.

“As soon as alpha-latrotoxin binds to specific receptors at the synapse (contacts between nerve cells or between nerve cells and muscles), calcium ions flow uncontrollably into the presynaptic membrane of the signal-transmitting cell.”

“This triggers the release of neurotransmitters, which causes strong muscle contractions and spasms.”

“Although this process seems simple at first glance, there are very complex mechanisms behind it.”

To better understand the mechanism of calcium influx into the presynaptic membrane, the authors used high-performance cryo-electron microscopy (cryo-EM) and molecular dynamics (MD) computer simulations.

They showed that alpha-latrotoxin undergoes significant changes when it binds to the receptor.

Some of the toxic molecules form stalks and penetrate the cell membrane like a syringe.

As a special feature, this stalk forms small pores in the membrane, which act as calcium channels.

MD simulations revealed that calcium ions can enter the cells through a selection gate on the side directly above the pore.

“This toxin mimics the function of calcium channels in the presynaptic membrane in a very complex way,” said Christos Gatsogiannis, a researcher at the University of Münster.

“Therefore, it is different in every way from any toxin known to date.”

“The new discovery opens up a wide range of potential applications.”

“Latrotoxin has considerable biotechnological potential, including the development of improved antidotes, treatments for paralysis, and new biopesticides.”

of study Published in a magazine nature communications.

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Clink BU others. 2024. Structural basis of α-latrotoxin transition to cation-selective pores. Nat Commune 15, 8551; doi: 10.1038/s41467-024-52635-5

Source: www.sci.news

Pharmacological potential discovered in toxins found in crustacean venom from Mayan underwater caves

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Xibalbanus turmensisThe poisonous remipede, found in the caves of Antiarin on the Yucatan Peninsula, is the only crustacean for which a venom system has been described.

Xibalbanus turmensis. Image credit: Pinheiro-Junior others., doi: 10.1186/s12915-024-01955-5.

“Poisonous animals inject toxic compounds into other organisms primarily for self-defense or predation,” said Dr. Björn von Roymont, a researcher at Goethe University Frankfurt, and his colleagues.

“Many venoms are composed of proteins that have evolved to modulate various physiological functions in the target organism.”

“Studying these biological activities could lead to pharmacological or agrochemical applications.”

“The majority of thoroughly studied venoms and venomous proteins originate from iconic terrestrial groups, primarily snakes, spiders, scorpions, and insects,” the researchers said.

“Research attention to marine life has been limited, with only a few fish and invertebrates being better studied, such as sea anemones, jellyfish, cone snails, cephalopods, polychaetes, and more recently nemertes.”

“Venoms and their toxic proteins have evolved independently in different animal lineages, so the study of new lineages provides an opportunity to identify novel toxic compounds with interesting biological activities, on the one hand, and generally convergent proteins on the other hand. It provides an opportunity to improve our understanding of the evolution of functional traits.”

In their study, the researchers investigated the biological activity of peptides found in crustacean venom. Xibalbanus turmensis.

This underwater cave-dwelling crustacean belongs to the following classes: Remipediafirst described in the 1980s and currently consists of 28 extant species.

“Xibalbanus turmensis They live in cenotes, underwater caves in Mexico's Yucatan Peninsula,” the scientists said.

“Cave dwellers directly inject the venom produced by their venom glands into their prey.”

“This toxin contains a variety of components, including a new type of peptide named cibalbin after the crustacean producer.”

“Some of these sibalbins contain characteristic structural elements that are well known to other toxins, especially those produced by spiders. Some amino acids (cysteine) in the peptide are tied together like a knot. are connected to each other in such a way that they form a structure.

“This makes the peptide more resistant to enzymes, heat, and extreme pH values.”

“Such knots often act as neurotoxins, interacting with ion channels to paralyze prey. This effect has also been proposed for some cibalbins.”

This study shows that all sibalbin peptides tested by the team, particularly Xib1, Xib2, and Xib13, effectively inhibit potassium channels in mammalian systems.

“This inhibition is very important when developing drugs to treat a variety of neurological diseases, including epilepsy,” Dr. von Roymont said.

“Xib1 and Xib13 also exhibit the ability to inhibit voltage-gated sodium channels, such as those found in neurons and cardiomyocytes.”

“Furthermore, in higher mammalian sensory neurons, the two peptides can activate two proteins involved in signal transduction: the kinases PKA-II and ERK1/2.”

“The latter suggests that they are involved in pain sensitization, opening the door to new approaches in pain treatment.”

of the team findings Published in a magazine BMC biology.

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EL Pinheiro – Junior others. 2024. Xibalbin mutants divergently evolved from remipede toxin inhibit potassium channels and activate PKA-II and Erk1/2 signaling. BMC biol 22, 164; doi: 10.1186/s12915-024-01955-5

Source: www.sci.news