cDNA cloning, structural, and functional analyses of venom phospholipases A2 and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii renardi

Tsai, Inn-Ho; Wang, Ying‐Ming; Cheng, An Chun; Starkov, Vladislav G.; Osipov, Alexey V.; Никитин, И. Г.; Makarova, Yana V.; Ziganshin, Rustam H.; Utkin, Yuri N.

doi:10.1016/j.toxicon.2010.12.012

Cited by 29 publications

(28 citation statements)

References 33 publications

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“…PLA 2 CM-II was purified from N. kaouthia venom as described [18] ; PLA 2 Vur-PL2 was isolated from V. ursinii venom as described [19] . The purity of the proteins was proved by analytical HPLC and mass spectrometry.…”

Section: Methodsmentioning

confidence: 99%

“…PLA 2 s vurtoxin and Vur-S49 were isolated from V. ursinii venom. For this purpose, crude venom was separated by gel-filtration as described [19] . Fraction 3+4 ( Figure 3A in [19] ) was further purified by reversed phase HPLC on a Discovery BIO Wide Pore C18 column (10×250 mm, Supelco) in a gradient of 25–40% (v/v) acetonitrile in 60 min in the presence of 0.1% (v/v) trifluoroacetic acid, at a flow rate of 2.0 ml/min ( Fig.…”

Section: Methodsmentioning

confidence: 99%

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Inhibition of Nicotinic Acetylcholine Receptors, a Novel Facet in the Pleiotropic Activities of Snake Venom Phospholipases A2

et al. 2014

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Phospholipases A2 represent the most abundant family of snake venom proteins. They manifest an array of biological activities, which is constantly expanding. We have recently shown that a protein bitanarin, isolated from the venom of the puff adder Bitis arietans and possessing high phospholipolytic activity, interacts with different types of nicotinic acetylcholine receptors and with the acetylcholine-binding protein. To check if this property is characteristic to all venom phospholipases A2, we have studied the capability of these enzymes from other snakes to block the responses of Lymnaea stagnalis neurons to acetylcholine or cytisine and to inhibit α-bungarotoxin binding to nicotinic acetylcholine receptors and acetylcholine-binding proteins. Here we present the evidence that phospholipases A2 from venoms of vipers Vipera ursinii and V. nikolskii, cobra Naja kaouthia, and krait Bungarus fasciatus from different snake families suppress the acetylcholine- or cytisine-elicited currents in L. stagnalis neurons and compete with α-bungarotoxin for binding to muscle- and neuronal α7-types of nicotinic acetylcholine receptor, as well as to acetylcholine-binding proteins. As the phospholipase A2 content in venoms is quite high, under some conditions the activity found may contribute to the deleterious venom effects. The results obtained suggest that the ability to interact with nicotinic acetylcholine receptors may be a general property of snake venom phospholipases A2, which add a new target to the numerous activities of these enzymes.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Inhibition of Nicotinic Acetylcholine Receptors, a Novel Facet in the Pleiotropic Activities of Snake Venom Phospholipases A2

et al. 2014

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“…Numerous snake venom sPLA 2 s that modulate platelet function have been characterized [13,14,15,16,17,18,19] and different mechanisms of action shown [6,15,20,21,22,23,24,25,26]. The sPLA 2 s effect on platelet aggregation can be independent or dependent on their catalytic activity.…”

Section: Introductionmentioning

confidence: 99%

Interactions of PLA2-s from Vipera lebetina, Vipera berus berus and Naja naja oxiana Venom with Platelets, Bacterial and Cancer Cells

Samel

Vija

Kurvet

et al. 2013

Toxins

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Secretory phospholipasesA2 (sPLA2s) form a large family of structurally related enzymes widespread in nature. Herein, we studied the inhibitory effects of sPLA2s from Vipera lebetina (VLPLA2), Vipera berus berus (VBBPLA2), and Naja naja oxiana (NNOPLA2) venoms on (i) human platelets, (ii) four different bacterial strains (gram-negative Escherichia coli and Vibrio fischeri; gram-positive Staphylococcus aureus and Bacillus subtilis) and (iii) five types of cancer cells (PC-3, LNCaP, MCF-7, K-562 and B16-F10) in vitro. sPLA2s inhibited collagen-induced platelet aggregation: VBBPLA2 IC50 = 0.054, VLPLA2 IC50 = 0.072, NNOPLA2 IC50 = 0.814 μM. p-Bromophenacylbromide-inhibited sPLA2 had no inhibitory action on platelets. 36.17 μM VBBPLA2 completely inhibited the growth of gram-positive Bacillus subtilis whereas no growth inhibition was observed towards gram-negative Escherichia coli. The inhibitory action of sPLA2s (~0.7 μM and ~7 μM) towards cancer cells depended on both venom and cell type. VBBPLA2 (7.2 μM) inhibited significantly the viability of K-562 cells and the cell death appeared apoptotic. The sPLA2s exhibited no inhibitory effect towards LNCaP cells and some effect (8%–20%) towards other cells. Thus, already sub-μM concentrations of sPLA2s inhibited collagen-induced platelet aggregation and from the current suite of studied svPLA2s and test cells, VBBPLA2 was the most growth inhibitory towards Bacillus subtilis and K-562 cells.

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“…AtnI 2 is probably endowed with a potent haemostatic activity based on 96% sequence identity with Vur-PL2 (ADG86231) from the closely related Russian snake V. renardi (former V. ursinii renardi). Vur-PL2 was namely described as a strongly anticoagulant and platelet aggregation inhibitory enzyme [34]. Although only weakly toxic in mice (LD 50 = 10.7 mg/kg), one third of experimental animals died from internal bleeding in various organs at an LD 50 dose of Vur-PL2.…”

Section: Discussionmentioning

confidence: 99%

Biological Activities and Proteomic Profile of the Venom of Vipera ursinii ssp., a very Rare Karst Viper from Croatia

Balija

Leonardi

Brgles

et al. 2020

Toxins

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The karst viper (Vipera ursinii ssp.) favours high-mountain dry grasslands in southern and south-eastern Croatia. It is medically less important than other Vipera species, because of its remote habitat and the very small amount of venom that it injects by its relatively short fangs. The scientific literature on Vipera ursinii deals mostly with the morphology, ecology and distribution range of this snake, due to the species’ conservation issues, while the toxinological aspects of its venom have not so far been investigated. Here we report on the composition and biological activity of the Vipera ursinii ssp. venom. Using a proteomics approach, we have identified 25 proteins in the venom that belong to seven protein families: snake venom metalloproteinase, serine protease, secreted phospholipase A2, cysteine-rich secretory protein, snake C-type lectin-like protein, serine protease inhibitor and nerve growth factor. The Vipera ursinii ssp. venom was found to be distinctively insecticidal. Its lethal toxicity towards crickets was more than five times greater than that of Vipera ammodytes ammodytes venom, while the opposite held in mice. Interestingly, the mode of dying after injecting a mouse with Vipera ursinii ssp. venom may suggest the presence of a neurotoxic component. Neurotoxic effects of European vipers have so far been ascribed exclusively to ammodytoxins and ammodytoxin-like basic secreted phospholipases A2. Structural and immunological analyses of the Vipera ursinii ssp. venom, however, confirmed that ammodytoxin-like proteins are not present in this venom.

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cDNA cloning, structural, and functional analyses of venom phospholipases A2 and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii renardi

Cited by 29 publications

References 33 publications

Inhibition of Nicotinic Acetylcholine Receptors, a Novel Facet in the Pleiotropic Activities of Snake Venom Phospholipases A2

Inhibition of Nicotinic Acetylcholine Receptors, a Novel Facet in the Pleiotropic Activities of Snake Venom Phospholipases A2

Interactions of PLA2-s from Vipera lebetina, Vipera berus berus and Naja naja oxiana Venom with Platelets, Bacterial and Cancer Cells

Biological Activities and Proteomic Profile of the Venom of Vipera ursinii ssp., a very Rare Karst Viper from Croatia

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