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.
“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
