Molecular insights into the powerful mucus-based adhesion of limpets (Patella vulgata L.).

Lengerer, Birgit 
Wattiez, Ruddy 
Flammang, Patrick 

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Limpets (Patella vulgata L.) are renowned for their powerful attachments to rocks on wave-swept seashores. Unlike adult barnacles and mussels, limpets do not adhere permanently; instead, they repeatedly transition between long-term adhesion and locomotive adhesion depending on the tide. Recent studies on the adhesive secretions (bio-adhesives) of marine invertebrates have expanded our knowledge on the composition and function of temporary and permanent bio-adhesives. In comparison, our understanding of the limpets' transitory adhesion remains limited. In this study, we demonstrate that suction is not the primary attachment mechanism in P. vulgata; rather, they secrete specialized pedal mucus for glue-like adhesion. Through combined transcriptomics and proteomics, we identified 171 protein sequences from the pedal mucus. Several of these proteins contain conserved domains found in temporary bio-adhesives from sea stars, sea urchins, marine flatworms and sea anemones. Many of these proteins share homology with fibrous gel-forming glycoproteins, including fibrillin, hemolectin and SCO-spondin. Moreover, proteins with potential protein- and glycan-degrading domains could have an immune defence role or assist degrading adhesive mucus to facilitate the transition from stationary to locomotive states. We also discovered glycosylation patterns unique to the pedal mucus, indicating that specific sugars may be involved in transitory adhesion. Our findings elucidate the mechanisms underlying P. vulgata adhesion and provide opportunities for future studies on bio-adhesives that form strong attachments and resist degradation until necessary for locomotion.

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Patellogastropoda, adhesive proteins, bio-adhesion, glycosylation, transitory adhesion, Animals, Behavior, Animal, Gastropoda, Gene Expression Profiling, Gene Regulatory Networks, Glycosylation, Locomotion, Mass Spectrometry, Mucus, Protein Domains, Proteomics, Sequence Analysis, RNA
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Open Biol
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The Royal Society
European Commission Horizon 2020 (H2020) Marie Sk?odowska-Curie actions (642861)