Chitin is a functional component of the larval adhesive of barnacles

Barnacles are the only sessile crustaceans, and their larva, the cyprid, is supremely adapted for attachment to surfaces. Barnacles have a universal requirement for strong adhesion at the point of larval attachment. Selective pressure on the cyprid adhesive has been intense and led to evolution of a...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Communications biology 2020-01, Vol.3 (1), p.31-31, Article 31
Hauptverfasser: Aldred, Nick, Chan, Vera Bin San, Emami, Kaveh, Okano, Keiju, Clare, Anthony S., Mount, Andrew S.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Barnacles are the only sessile crustaceans, and their larva, the cyprid, is supremely adapted for attachment to surfaces. Barnacles have a universal requirement for strong adhesion at the point of larval attachment. Selective pressure on the cyprid adhesive has been intense and led to evolution of a tenacious and versatile natural glue. Here we provide evidence that carbohydrate polymers in the form of chitin provide stability to the cyprid adhesive of Balanus amphitrite . Chitin was identified surrounding lipid-rich vesicles in the cyprid cement glands. The functional role of chitin was demonstrated via removal of freshly attached cyprids from surfaces using a chitinase. Proteomic analysis identified a single cement gland-specific protein via its association with chitin and localized this protein to the same vesicles. The role of chitin in cyprid adhesion raises intriguing questions about the evolution of barnacle adhesion, as well as providing a new target for antifouling technologies. Nick Aldred et al. show that chitin provides stability in the cyprid adhesive of the barnacle Balanus amphitrite . They show that a single cement gland-specific protein associates with chitin, and that freshly attached cyprids can be removed from surfaces using chitinase.
ISSN:2399-3642
2399-3642
DOI:10.1038/s42003-020-0751-5