ArticleProceedings. Biological sciences2010
Harnessing disorder: onychophorans use highly unstructured proteins, not silks, for prey capture.
Article in Proceedings. Biological sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 53 citations in OpenAlex.
- Triangle weaver spiders construct spring-loaded webs using a novel set of genes for exceptionally proline-rich silk.PNAS nexus · 2025Article
- Evolutionary Insights into the Length Variation of DNA Damage Response Proteins Across Eukaryotes.Genome biology and evolution · 2025Article
- Conserved leucine-rich repeat proteins in the adhesive projectile slime of velvet worms.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phase separation and ageing of glycine-rich protein from tick adhesive.Nature chemistry · 2025Article
- Proton conductivity of the protein-based velvet worm slime.iScience · 2024Article
- Recurrent evolution of adhesive defence systems in amphibians by parallel shifts in gene expression.Nature communications · 2024Article
- The venom and telopodal defence systems of the centipede Lithobius forficatus are functionally convergent serial homologues.BMC biology · 2024Article
- Peculiar Phosphonate Modifications of Velvet Worm Slime Revealed by Advanced Nuclear Magnetic Resonance and Mass Spectrometry.Journal of the American Chemical Society · 2023Article
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Sizing Up the Onychophoran Genome: Repeats, Introns, and Gene Family Expansion Contribute to Genome Gigantism in Epiperipatus broadwayi.Genome biology and evolution · 2023Article
- Encapsulated salts in velvet worm slime drive its hardening.Scientific reports · 2022Article
- Complete Sequences of the Velvet Worm Slime Proteins Reveal that Slime Formation is Enabled by Disulfide Bonds and Intrinsically Disordered Regions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Low complexity regions in the proteins of prokaryotes perform important functional roles and are highly conserved.Nucleic acids research · 2019Article
- Fingerprinting of Proteins that Mediate Quagga Mussel Adhesion using a De Novo Assembled Foot Transcriptome.Scientific reports · 2019Article
- Mechanoresponsive lipid-protein nanoglobules facilitate reversible fibre formation in velvet worm slime.Nature communications · 2017Article
- An option space for early neural evolution.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Oscillation of the velvet worm slime jet by passive hydrodynamic instability.Nature communications · 2015Article
- Experimental strategies for the identification and characterization of adhesive proteins in animals: a review.Interface focus · 2015Review
- Identification of proteins associated with adhesive prints from Holothuria dofleinii Cuvierian tubules.Marine biotechnology (New York, N.Y.) · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Onychophora are ancient, carnivorous soft-bodied invertebrates which capture their prey in slime that originates from dedicated glands located on either side of the head. While the biochemical composition of the slime is known, its unusual nature and the mechanism of ensnaring thread formation have remained elusive. We have examined gene expression in the slime gland from an Australian onychophoran, Euperipatoides rowelli, and matched expressed sequence tags to separated proteins from the slime. The analysis revealed three categories of protein present: unique high-molecular-weight proline-rich proteins, and smaller concentrations of lectins and small peptides, the latter two likely to act as protease inhibitors and antimicrobial agents. The predominant proline-rich proteins (200 kDa+) are composed of tandem repeated motifs and distinguished by an unusually high proline and charged residue content. Unlike the highly structured proteins such as silks used for prey capture by spiders and insects, these proteins lack ordered secondary structure over their entire length. We propose that on expulsion of slime from the gland onto prey, evaporative water loss triggers a glass transition change in the protein solution, resulting in adhesive and enmeshing thread formation, assisted by cross-linking of complementary charged and hydrophobic regions of the protein. Euperipatoides rowelli has developed an entirely new method of capturing prey by harnessing disordered proteins rather than structured, silk-like proteins.
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