Phospholipase A2 from the venom of the spider Eresus niger

Atakuziev, B. U.; Nuritova, F. A.; Usmanov, P. B.

doi:10.1007/bf00636578

Cited by 3 publications

(3 citation statements)

References 3 publications

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“…Phospholipases A2 cleaves glycerophospholipids, membrane components, generating lysophospholipids and fatty acids that compose the venom of snakes, scorpions, spiders, bees, corals, and sea anemones [ 51 , 52 , 53 , 54 , 55 , 56 ]. One phospholipase A2 was identified, but did not share higher similarity to the phospholipase A2, already characterized from B. caissarum ’s, phospholipase A2 Bcs-2a.…”

Section: Discussionmentioning

confidence: 99%

Multiomic Approach for Bioprospection: Investigation of Toxins and Peptides of Brazilian Sea Anemone Bunodosoma caissarum

et al. 2023

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Sea anemones are sessile invertebrates of the phylum Cnidaria and their survival and evolutive success are highly related to the ability to produce and quickly inoculate venom, with the presence of potent toxins. In this study, a multi-omics approach was applied to characterize the protein composition of the tentacles and mucus of Bunodosoma caissarum, a species of sea anemone from the Brazilian coast. The tentacles transcriptome resulted in 23,444 annotated genes, of which 1% showed similarity with toxins or proteins related to toxin activity. In the proteome analysis, 430 polypeptides were consistently identified: 316 of them were more abundant in the tentacles while 114 were enriched in the mucus. Tentacle proteins were mostly enzymes, followed by DNA- and RNA-associated proteins, while in the mucus most proteins were toxins. In addition, peptidomics allowed the identification of large and small fragments of mature toxins, neuropeptides, and intracellular peptides. In conclusion, integrated omics identified previously unknown or uncharacterized genes in addition to 23 toxin-like proteins of therapeutic potential, improving the understanding of tentacle and mucus composition of sea anemones.

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Section: Discussionmentioning

confidence: 99%

Multiomic Approach for Bioprospection: Investigation of Toxins and Peptides of Brazilian Sea Anemone Bunodosoma caissarum

et al. 2023

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“…Phospholipases A2 (PLA2) have already been described in various Hymenoptera (Apis spp., Bombus terrestris) but also in snake and spider venoms [20,43] and act as neuro-and myotoxins by hydrolyzing membrane phospholipids of motor nerves and subsequently leading to cell lysis [20]. Here, two different isoforms with a sequence identity of 99% are reported in PDV and one of these isoforms in YJV.…”

Section: Identifiermentioning

confidence: 98%

Shedding Light on the Venom Proteomes of the Allergy-Relevant Hymenoptera Polistes dominula (European Paper Wasp) and Vespula spp. (Yellow Jacket)

Grosch

Hilger

Bilò

et al. 2020

Toxins

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Allergic reactions to stings of Hymenoptera species can have serious or even fatal consequences. If the identification of the culprit insect is possible, venom-specific immunotherapy effectively cures Hymenoptera venom allergies. Although component-resolved diagnostics has strongly evolved in recent years, the differentiation between allergies to closely related species such as Polistes dominula and Vespula spp. is still challenging. In order to generate the basis for new diagnostic and therapeutic strategies, this study aims at resolving the venom proteomes (venomes) of these species. The venoms of P. dominula and Vespula spp. (V. germanica, V. vulgaris) were analyzed by liquid chromatography-mass spectrometry. Resulting proteins were characterized regarding their function, localization and biochemical properties. The analyses yielded 157 proteins in Vespula spp. and 100 in P. dominula venom; 48 proteins, including annotated allergens, were found in both samples. In addition to a variety of venom trace molecules, new allergen candidates such as icarapin-like protein and phospholipase A2 were identified. This study elucidates the venomes of closely related allergy-eliciting Hymenoptera species. The data indicates that relying on marker allergens to differentiate between P. dominula and Vespula spp. venom allergy is probably insufficient and that strategies using cross-reactive major allergens could be more promising.

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“…This protein has not only been described as a major allergen, but also leads to, e.g., cell lysis, pore formation, platelet aggregation and hemolysis due to its enzymatic effects [ 20 , 21 ]. In addition to PLA1, PLA2 also plays a role in various venomous spiders, snakes and Hymenoptera ( A. mellifera, Apis cerana, Bombus terrestris ) [ 22 , 23 , 24 ]. PLA2 is a Ca 2+ -dependent, secreted phospholipase, which hydrolyzes membrane phospholipids of motor nerves and thereby induces cell lysis.…”

Section: Introductionmentioning

confidence: 99%

Characterization of New Allergens from the Venom of the European Paper Wasp Polistes dominula

Grosch

Eberlein

Waldherr

et al. 2021

Toxins

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Discriminating Polistes dominula and Vespula spp. venom allergy is of growing importance worldwide, as systemic reactions to either species’ sting can lead to severe outcomes. Administering the correct allergen-specific immunotherapy is therefore a prerequisite to ensure the safety and health of venom-allergic patients. Component-resolved diagnostics of Hymenoptera venom allergy might be improved by adding additional allergens to the diagnostic allergen panel. Therefore, three potential new allergens from P. dominula venom—immune responsive protein 30 (IRP30), vascular endothelial growth factor C (VEGF C) and phospholipase A2 (PLA2)—were cloned, recombinantly produced and biochemically characterized. Sera sIgE titers of Hymenoptera venom-allergic patients were measured in vitro to assess the allergenicity and potential cross-reactivity of the venom proteins. IRP30 and VEGF C were classified as minor allergens, as sensitization rates lay around 20–40%. About 50% of P. dominula venom-allergic patients had measurable sIgE titers directed against PLA2 from P. dominula venom. Interestingly, PLA2 was unable to activate basophils of allergic patients, questioning its role in the context of clinically relevant sensitization. Although the obtained results hint to a questionable benefit of the characterized P. dominula venom proteins for improved diagnosis of venom-allergic patients, they can contribute to a deeper understanding of the molecular mechanisms of Hymenoptera venoms and to the identification of factors that determine the allergenic potential of proteins.

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Phospholipase A2 from the venom of the spider Eresus niger

Cited by 3 publications

References 3 publications

Multiomic Approach for Bioprospection: Investigation of Toxins and Peptides of Brazilian Sea Anemone Bunodosoma caissarum

Multiomic Approach for Bioprospection: Investigation of Toxins and Peptides of Brazilian Sea Anemone Bunodosoma caissarum

Shedding Light on the Venom Proteomes of the Allergy-Relevant Hymenoptera Polistes dominula (European Paper Wasp) and Vespula spp. (Yellow Jacket)

Characterization of New Allergens from the Venom of the European Paper Wasp Polistes dominula

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