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"Venom."
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Venom : poisonous creatures in the natural world
Poison is an everyday part of the animal world, and an essential tool for hunting and defence. A wide variety of insects, reptiles and amphibians use toxins to subdue their prey or to stop becoming prey to another predator. Even some mammals and birds resort to poison as a means of securing a meal or deterring attack! From the nine-feet long Komodo Dragon through species such as the King Cobra, Lionfish, Fat-tail Scorpion and Poison Dart-frog to the diminutive but lethal Black Widow Spider, author Steve Backshall takes a fascinating look at the different types of natural venoms. On a tour of the world's continents, he looks at over 60 of the most venomous creatures, describing their main characteristics and explaining how they administer their venom and what its effects are. Colour photographs and exciting accounts of Steve's own encounters with some of these animals bring the world of natural venom alive. He also looks at the science of natural toxins, and at how natural venoms are increasingly used in medicine and for the treatment of chronic disease in humans.
Book
Updated Nematocyst Types in Tentacle of Venomous Box Jellyfish, Chironex indrasaksajiae sub. in Thai Waters
The multiple-tentacle box jellyfish, Chironex indrasaksajiae (Sucharitakul, 2017) and Chiropsoides buitendijki (Horst, 1907), are venomous species found in Thai waters. They are responsible for numerous envenomations through their stinging organelles, nematocysts. These specialized microscopic structures discharge venom, yet detailed knowledge of their types and morphology in these species remains limited. This study updates the characterization of nematocyst types and features in C. indrasaksajiae and C. buitendijki using light and scanning electron microscopy for detailed examination. Four distinct nematocyst types were identified: banana-shaped microbasic p-mastigophores, oval-shaped microbasic p-rhopaloids, sub-spherical microbasic p-rhopaloids, and rod-shaped isorhizas. In C. indrasaksajiae, banana-shaped microbasic p-mastigophores exhibited significant intraspecific variability, ranging from 30.26 µm to 102.56 µm in length and 6.42 µm to 17.01 µm in width. Conversely, C. buitendijki showed a narrower size range, 72.17 µm to 98.37 µm in length and 10.73 µm to 16.48 µm in width, based on multiple individuals. The size ranges for the other nematocyst types were consistent across both species. This study enhances the understanding of nematocyst morphology in these box jellyfish, providing a foundation for further research on venom delivery mechanisms and improved management of jellyfish envenomations in Thai waters.
Journal Article
Deadly venomous mammals!
\"Learn all about rare venomous mammals in this engrossing new narrative nonfiction book for young readers. It's packed with exciting wildlife encounters, cutting-edge science, and loads of info about venom and its deadly effects\"-- Provided by publisher.
Book
De novo designed proteins neutralize lethal snake venom toxins
Snakebite envenoming remains a devastating and neglected tropical disease, claiming over 100,000 lives annually and causing severe complications and long-lasting disabilities for many more
1
,
2
. Three-finger toxins (3FTx) are highly toxic components of elapid snake venoms that can cause diverse pathologies, including severe tissue damage
3
and inhibition of nicotinic acetylcholine receptors, resulting in life-threatening neurotoxicity
4
. At present, the only available treatments for snakebites consist of polyclonal antibodies derived from the plasma of immunized animals, which have high cost and limited efficacy against 3FTxs
5
,
6
–
7
. Here we used deep learning methods to de novo design proteins to bind short-chain and long-chain α-neurotoxins and cytotoxins from the 3FTx family. With limited experimental screening, we obtained protein designs with remarkable thermal stability, high binding affinity and near-atomic-level agreement with the computational models. The designed proteins effectively neutralized all three 3FTx subfamilies in vitro and protected mice from a lethal neurotoxin challenge. Such potent, stable and readily manufacturable toxin-neutralizing proteins could provide the basis for safer, cost-effective and widely accessible next-generation antivenom therapeutics. Beyond snakebite, our results highlight how computational design could help democratize therapeutic discovery, particularly in resource-limited settings, by substantially reducing costs and resource requirements for the development of therapies for neglected tropical diseases.
Deep learning methods have been used to design proteins that can neutralize the effects of three-finger toxins found in snake venom, which could lead to the development of safer and more accessible antivenom treatments.
Journal Article
Venom : the secrets of nature's deadliest weapon
\"The story of venom from ancient origins to modern medicinal use\"-- Provided by publisher.
Book
In vitro assessment and phase I randomized clinical trial of anfibatide a snake venom derived anti-thrombotic agent targeting human platelet GPIbα
The interaction of platelet GPIbα with von Willebrand factor (VWF) is essential to initiate platelet adhesion and thrombosis, particularly under high shear stress conditions. However, no drug targeting GPIbα has been developed for clinical practice. Here we characterized anfibatide, a GPIbα antagonist purified from snake (
Deinagkistrodon acutus
) venom, and evaluated its interaction with GPIbα by surface plasmon resonance and in silico modeling. We demonstrated that anfibatide interferds with both VWF and thrombin binding, inhibited ristocetin/botrocetin- and low-dose thrombin-induced human platelet aggregation, and decreased thrombus volume and stability in blood flowing over collagen. In a single-center, randomized, and open-label phase I clinical trial, anfibatide was administered intravenously to 94 healthy volunteers either as a single dose bolus, or a bolus followed by a constant rate infusion of anfibatide for 24 h. Anfibatide inhibited VWF-mediated platelet aggregation without significantly altering bleeding time or coagulation. The inhibitory effects disappeared within 8 h after drug withdrawal. No thrombocytopenia or anti-anfibatide antibodies were detected, and no serious adverse events or allergic reactions were observed during the studies. Therefore, anfibatide was well-tolerated among healthy subjects. Interestingly, anfibatide exhibited pharmacologic effects in vivo at concentrations thousand-fold lower than in vitro, a phenomenon which deserves further investigation.
Trial registration:
Clinicaltrials.gov NCT01588132.
Journal Article
Deadly animal poisons
Describes how different animals use poison to capture prey and escape predators.
Book
Proteomics and antivenomics of Echis carinatus carinatus venom: Correlation with pharmacological properties and pathophysiology of envenomation
The proteome composition of
Echis carinatus carinatus
venom (ECV) from India was studied for the first time by tandem mass spectrometry analysis. A total of 90, 47, and 22 distinct enzymatic and non-enzymatic proteins belonging to 15, 10, and 6 snake venom protein families were identified in ECV by searching the ESI-LC-MS/MS data against non-redundant protein databases of Viperidae (taxid 8689),
Echis
(taxid 8699) and
Echis carinatus
(taxid 40353), respectively. However, analysis of MS/MS data against the Transcriptome Shotgun Assembly sequences (87 entries) of conger
E
.
coloratus
identified only 14 proteins in ECV. Snake venom metalloproteases and snaclecs, the most abundant enzymatic and non-enzymatic proteins, respectively in ECV account for defibrinogenation and the strong
in vitro
pro-coagulant activity. Further, glutaminyl cyclase, aspartic protease, aminopeptidase, phospholipase B, vascular endothelial growth factor, and nerve growth factor were reported for the first time in ECV. The proteome composition of ECV was well correlated with its biochemical and pharmacological properties and clinical manifestations observed in
Echis
envenomed patients. Neutralization of enzymes and pharmacological properties of ECV, and immuno-cross-reactivity studies unequivocally point to the poor recognition of <20 kDa ECV proteins, such as PLA
2
, subunits of snaclec, and disintegrin by commercial polyvalent antivenom.
Journal Article
Poison! : the spitting cobra and other venomous animals
Learn about venomous snakes and other poisonous animals.
Book
The Diversity of Venom: The Importance of Behavior and Venom System Morphology in Understanding Its Ecology and Evolution
Venoms are one of the most convergent of animal traits known, and encompass a much greater taxonomic and functional diversity than is commonly appreciated. This knowledge gap limits the potential of venom as a model trait in evolutionary biology. Here, we summarize the taxonomic and functional diversity of animal venoms and relate this to what is known about venom system morphology, venom modulation, and venom pharmacology, with the aim of drawing attention to the importance of these largely neglected aspects of venom research. We find that animals have evolved venoms at least 101 independent times and that venoms play at least 11 distinct ecological roles in addition to predation, defense, and feeding. Comparisons of different venom systems suggest that morphology strongly influences how venoms achieve these functions, and hence is an important consideration for understanding the molecular evolution of venoms and their toxins. Our findings also highlight the need for more holistic studies of venom systems and the toxins they contain. Greater knowledge of behavior, morphology, and ecologically relevant toxin pharmacology will improve our understanding of the evolution of venoms and their toxins, and likely facilitate exploration of their potential as sources of molecular tools and therapeutic and agrochemical lead compounds.
Journal Article