Heterodimeric V. nikolskii phospholipases A2 induce aggregation of the lipid bilayer

Алексеева, А. С.; Tretiakova, Daria; Chernikov, Valery P.; Utkin, Yuri N.; Molotkovsky, Julian G.; Водовозова, Е. Л.; Болдырев, Иван

doi:10.1016/j.toxicon.2017.05.015

Cited by 12 publications

(6 citation statements)

References 41 publications

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“…However, V. kaznakovi had a higher percentage of PLA 2 and SVSP compared to V. anatolica (46,66). V. nikolskii, V. orlovi, V. renardii, and V. kaznakovi were all reported to have greater PLA 2 percentage compared to other toxins followed by SVMPs (67)(68)(69). Great diversity may exist within each of these toxin classes.…”

Section: Discussionmentioning

confidence: 94%

Venom-Induced Blood Disturbances by Palearctic Viperid Snakes, and Their Relative Neutralization by Antivenoms and Enzyme-Inhibitors

et al. 2021

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Palearctic vipers are medically significant snakes in the genera Daboia, Macrovipera, Montivipera, and Vipera which occur throughout Europe, Central Asia, Near and Middle East. While the ancestral condition is that of a small-bodied, lowland species, extensive diversification has occurred in body size, and niche specialization. Using 27 venom samples and a panel of in vitro coagulation assays, we evaluated the relative coagulotoxic potency of Palearctic viper venoms and compared their neutralization by three antivenoms (Insoserp Europe, VIPERFAV and ViperaTAb) and two metalloprotease inhibitors (prinomastat and DMPS). We show that variation in morphology parallels variation in the Factor X activating procoagulant toxicity, with the three convergent evolutions of larger body sizes (Daboia genus, Macrovipera genus, and Vipera ammodytes uniquely within the Vipera genus) were each accompanied by a significant increase in procoagulant potency. In contrast, the two convergent evolutions of high altitude specialization (the Montivipera genus and Vipera latastei uniquely within the Vipera genus) were each accompanied by a shift away from procoagulant action, with the Montivipera species being particularly potently anticoagulant. Inoserp Europe and VIPERFAV antivenoms were both effective against a broad range of Vipera species, with Inoserp able to neutralize additional species relative to VIPERFAV, reflective of its more complex antivenom immunization mixture. In contrast, ViperaTAb was extremely potent in neutralizing V. berus but, reflective of this being a monovalent antivenom, it was not effective against other Vipera species. The enzyme inhibitor prinomastat efficiently neutralized the metalloprotease-driven Factor X activation of the procoagulant venoms. In contrast, DMPS (2,3-dimercapto-1-propanesulfonic acid), which as been suggested as another potential treatment option in the absence of antivenom, DMPS failed against all venoms tested. Overall, our results highlight the evolutionary variations within Palearctic vipers and help to inform clinical management of viper envenomation.

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Section: Discussionmentioning

confidence: 94%

Venom-Induced Blood Disturbances by Palearctic Viperid Snakes, and Their Relative Neutralization by Antivenoms and Enzyme-Inhibitors

et al. 2021

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“…Thus, depending on the origin, and, therefore, the composition of the envelope, PLA 2 s can differently affect the viruses and exert different virucidal activities. Interestingly, it was recently shown that HDP-2 induced an aggregation and stacking of lipid bilayers [65].…”

Section: Discussionmentioning

confidence: 99%

Snake venom phospholipase A2s exhibit strong virucidal activity against SARS-CoV-2 and inhibit the viral spike glycoprotein interaction with ACE2

Siniavin

Streltsova

Никифорова

et al. 2021

Cell. Mol. Life Sci.

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“…The reaction of the lipid bilayer to enzyme binding was also studied. For example, heterodimeric PLA2 from the venom of Nikolsky's viper induces aggregation of the lipid bilayer and the formation of multilayer lipid particles [12]. Embedding into the membrane of PLA2 from the bee venom causes the formation of depressions on the membrane surface leading to the appearance of a hydrophobic mismatch between the bilayer regions in the contact zone and beyond, which results in the displacement of phospholipid heads from the area of contact with the protein (formation of a hydrophobic spot) and thinning of the bilayer [13].…”

Section: Short Communicationmentioning

confidence: 99%

Estimation of the Phospholipase A2 Selectivity on POPC/POPG Membranes Using the Interaction Map

Алексеева

Volynsky

Болдырев

2021

Biochem. Moscow Suppl. Ser. A

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The regulation of the activity and selectivity of phospholipase A2 (PLA2), which is capable of cleaving fatty acid in the second position (sn-2) of the phospholipid, is carried out through the membrane-binding and catalytic sites of the enzyme. For hydrolytic activity, PLA2 must first bind to the phospholipid membrane, and the binding efficiency depends on the composition of the membrane. The membrane-binding site of PLA2 is formed by several tens of amino acids and its composition differs from enzyme to enzyme; hydrophobic and positively charged amino acids play a key role in the interaction. In this work, we investigated the interaction of PLA2 from bee venom with phospholipid bilayers of palmitoyl oleoylphosphatidylcholine (POPC) containing different amounts of palmitoyloleoylphosphatidylglycerol (POPG). On the basis of the measurements of the protein intrinsic fluorescence and the anisotropy of the fluorescence of the lipid probe we propose the construction of lipid–protein interaction maps, which reflect both the efficiency of protein binding and changes in the structure of the membrane. These changes cause alterations in the fluorescence anisotropy of the label, which in turn is a measure of the mobility of the lipid environment of the fluorescent probe. Analysis of interaction maps showed that there is a relationship between lipid mobility and enzyme binding efficiency: the optimum interaction of PLA2 with membranes from a POPC/POPG mixture lies in the region of the highest lipid mobility, and not in the region of the highest negative charge. This dependence complements the existing understanding of the process of recognition of the membrane surface by the enzyme and the selection of lipids by the enzyme already bound to the membrane. The proposed mapping method can be extended to other membrane-active proteins.

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Heterodimeric V. nikolskii phospholipases A2 induce aggregation of the lipid bilayer

Cited by 12 publications

References 41 publications

Venom-Induced Blood Disturbances by Palearctic Viperid Snakes, and Their Relative Neutralization by Antivenoms and Enzyme-Inhibitors

Venom-Induced Blood Disturbances by Palearctic Viperid Snakes, and Their Relative Neutralization by Antivenoms and Enzyme-Inhibitors

Snake venom phospholipase A2s exhibit strong virucidal activity against SARS-CoV-2 and inhibit the viral spike glycoprotein interaction with ACE2

Estimation of the Phospholipase A2 Selectivity on POPC/POPG Membranes Using the Interaction Map

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