ArticleThe Journal of biological chemistry2015
Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 49 citations in OpenAlex.
- Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Proteome Analysis of the Six-Eyed Sand-SpiderToxins · 2025Article
- Article
- Review
- Enlightening the toxinological dark matter of spider venom enzymes.npj biodiversity · 2024Article
- A Brief Overview of the Toxic Sphingomyelinase Ds of Brown Recluse Spider Venom and Other Organisms and Simple Methods To Detect Production of Its Signature Cyclic Ceramide Phosphate.Molecular pharmacology · 2024Article
- Comparative Biochemical, Structural, and Functional Analysis of Recombinant Phospholipases D from ThreeInternational journal of molecular sciences · 2023Article
- Protein salvage and repurposing in evolution: Phospholipase D toxins are stabilized by a remodeled scrap of a membrane association domain.Protein science : a publication of the Protein Society · 2023Article
- Lysophosphatidylglycerol (LPG) phospholipase D maintains membrane homeostasis in Staphylococcus aureus by converting LPG to lysophosphatidic acid.The Journal of biological chemistry · 2023Article
- Digestive enzymes and sphingomyelinase D in spiders without venom (Uloboridae).Scientific reports · 2023Article
- Article
- Specificity of Loxosceles α clade phospholipase D enzymes for choline-containing lipids: Role of a conserved aromatic cage.PLoS computational biology · 2022Article
- Evaluation of the effects ofToxicology reports · 2022Article
- Switching the substrate specificity of lysoplasmalogen-specific phospholipase D.FEBS open bio · 2021Article
- Pain-related toxins in scorpion and spider venoms: a face to face with ion channels.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Article
- Loxoscelism: Advances and Challenges in the Design of Antibody Fragments with Therapeutic Potential.Toxins · 2020Article
- Review
- Evolutionary dynamics of origin and loss in the deep history of phospholipase D toxin genes.BMC evolutionary biology · 2018Article
- The Role of Disulfide Bond Replacements in Analogues of the Tarantula Toxin ProTx-II and Their Effects on Inhibition of the Voltage-Gated Sodium Ion Channel NaJournal of the American Chemical Society · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Venoms of the sicariid spiders contain phospholipase D enzyme toxins that can cause severe dermonecrosis and even death in humans. These enzymes convert sphingolipid and lysolipid substrates to cyclic phosphates by activating a hydroxyl nucleophile present in both classes of lipid. The most medically relevant substrates are thought to be sphingomyelin and/or lysophosphatidylcholine. To better understand the substrate preference of these toxins, we used (31)P NMR to compare the activity of three related but phylogenetically diverse sicariid toxins against a diverse panel of sphingolipid and lysolipid substrates. Two of the three showed significantly faster turnover of sphingolipids over lysolipids, and all three showed a strong preference for positively charged (choline and/or ethanolamine) over neutral (glycerol and serine) headgroups. Strikingly, however, the enzymes vary widely in their preference for choline, the headgroup of both sphingomyelin and lysophosphatidylcholine, versus ethanolamine. An enzyme from Sicarius terrosus showed a strong preference for ethanolamine over choline, whereas two paralogous enzymes from Loxosceles arizonica either preferred choline or showed no significant preference. Intrigued by the novel substrate preference of the Sicarius enzyme, we solved its crystal structure at 2.1 Å resolution. The evolution of variable substrate specificity may help explain the reduced dermonecrotic potential of some natural toxin variants, because mammalian sphingolipids use primarily choline as a positively charged headgroup; it may also be relevant for sicariid predatory behavior, because ethanolamine-containing sphingolipids are common in insect prey.
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Registered trials
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