ArticleScientific reports2023
Digestive enzymes and sphingomyelinase D in spiders without venom (Uloboridae).
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Exploring Spiders Without Venom as New Sources of Peptidase Inhibitors.International journal of molecular sciences · 2025Article
- Molecular Mechanisms of Venom Diversity.Toxins · 2025Review
- Digestion in the arachnid Mischonyx squalidus as a probable source of lipids to synthesize opiliones defense and communication molecules.Scientific reports · 2025Article
- Beyond venomous fangs: Uloboridae spiders have lost their venom but not their toxicity.BMC biology · 2025Article
- Spider venom potency exhibits phylogenetic prey specificity but does not trade-off with body size or silk use in prey capture.Biology letters · 2025Article
- Article
- Enlightening the toxinological dark matter of spider venom enzymes.npj biodiversity · 2024Article
- Diversity and Functionality of Bacteria Associated with Different Tissues of Spider Heteropoda venatoria Revealed through Integration of High-Throughput Sequencing and Culturomics Approaches.Microbial ecology · 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
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spiders have distinct predatory behaviours selected along Araneae's evolutionary history but are mainly based on the use of venom for prey paralysis. Uloboridae spiders have lost their venom glands secondarily during evolution. Because of this, they immobilise their prey by extensively wrapping, and digestion starts with the addition of digestive fluid. During the extra-oral digestion, the digestive fluid liquefies both the prey and the AcSp2 spidroins from the web fibres. Despite the efficiency of this process, the cocktail of enzymes involved in digestion in Uloboridae spiders remains unknown. In this study, the protein content in the midgut of Uloborus sp. was evaluated through enzymatic, proteomic, and phylogenetic analysis. Hydrolases such as peptidases (endo and exopeptidases: cysteine, serine, and metallopeptidases), carbohydrases (alpha-amylase, chitinase, and alpha-mannosidase), and lipases were biochemically assayed, and 50 proteins (annotated as enzymes, structural proteins, and toxins) were identified, evidencing the identity between the digestive enzymes present in venomous and non-venomous spiders. Even enzymes thought to be unique to venom, including enzymes such as sphingomyelinase D, were found in the digestive system of non-venomous spiders, suggesting a common origin between digestive enzymes and enzymes present in venoms. This is the first characterization of the molecules involved in the digestive process and the midgut protein content of a non-venomous spider.
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