Structural assembly of the glycan-rich, chitin-reinforced adhesive of Hydra is coordinated by a lectin-like protein, HvAb1

Aquatic animals deploy adhesives, in numerous essential functions, and reversibility is a key adaptation. The molecular mechanisms of reversible wet adhesion remain poorly understood. Using a model organism, the freshwater cnidarian Hydra vulgaris, we dissect the mechanism of molecular assembly in a secreted adhesive and uncover a glycan and protein-based architecture organized by a lectin-like protein, Hydra vulgaris adhesive protein 1 (HvAb1). We identify HvAb1 as a nonredundant organizer of the adhesive matrix, being basal-disc specific and secreted. Knockdown of HvAb1 severely impaired attachment and disrupted footprint architecture in a mosaic pattern, with only HvAb1-positive regions o