ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 104 citations in OpenAlex.
- Spider venom peptides Ht1a and Gg1a are toxic to honeybee parasitenpj drug discovery · 2026Article
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides.Cellular and molecular life sciences : CMLS · 2026Article
- Ancient origin and dynamic evolution of bivalent spider toxins.Molecular biology and evolution · 2026Article
- Web of Potentials: Neuroactive Components of Spider Venom and Their Emerging Pharmacologic Applications in Neurologic Diseases.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- The green lacewing venom system and the complex mechanisms underlying its evolution.Molecular biology and evolution · 2026Article
- Review
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Genome of venomous caterpillarProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular Mechanisms of Venom Diversity.Toxins · 2025Review
- Comparative venomics suggests an evolutionary adaption of spider venom from predation to defense.Communications biology · 2025Article
- Duplication of a conserved mitochondrial enzyme gene arms parasitoid wasps with venom cytotoxicity and oogenesis regulation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Spider venom peptides with unique fold selectively block Shaker-type potassium channels.Cellular and molecular life sciences : CMLS · 2025Article
- A large language model for predicting neurotoxic peptides and neurotoxins.Protein science : a publication of the Protein Society · 2025Article
- Structural analysis of an Asterias rubens peptide indicates the presence of a disulfide-directed β-hairpin fold.FEBS open bio · 2025Article
- Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025Article
- Transgenic tomato strategies targeting whitefly eggs from apoplastic or ovary-directed proteins.BMC plant biology · 2024Article
- Unveiling Diversity and Function: Venom-Associated Microbes in Two Spiders, Heteropoda venatoria and Chilobrachys guangxiensis.Microbial ecology · 2024Article
- A Tachyplesin Antimicrobial Peptide from Theraphosidae Spiders with Potent Antifungal Activity AgainstMicroorganisms · 2024Article
- Enlightening the toxinological dark matter of spider venom enzymes.npj biodiversity · 2024Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spiders are one of the most successful venomous animals, with more than 48,000 described species. Most spider venoms are dominated by cysteine-rich peptides with a diverse range of pharmacological activities. Some spider venoms contain thousands of unique peptides, but little is known about the mechanisms used to generate such complex chemical arsenals. We used an integrated transcriptomic, proteomic, and structural biology approach to demonstrate that the lethal Australian funnel-web spider produces 33 superfamilies of venom peptides and proteins. Twenty-six of the 33 superfamilies are disulfide-rich peptides, and we show that 15 of these are knottins that contribute >90% of the venom proteome. NMR analyses revealed that most of these disulfide-rich peptides are structurally related and range in complexity from simple to highly elaborated knottin domains, as well as double-knot toxins, that likely evolved from a single ancestral toxin gene.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.