A molecular model of sea urchin reversible adhesion based on quantitative proteomics

Marine bioadhesives have unmatched performances especially in wet environments, being valuable sources of inspiration for industrial and biomedical applications. In sea urchins specialized adhesive organs, called tube feet, mediate adhesion. These are composed by a disc, which produces adhesive and de-adhesive secretions for strong reversible attachment, and a motile stem. After detachment, the secreted adhesive remains bound to the substratum as a footprint. Previous studies showed that sea urchin adhesive is composed of proteins and sugars, but so far only one protein, Nectin, was shown to be over-expressed as a transcript in tube feet discs, suggesting its involvement in sea urchin adhesion. Here we use high-resolution quantitative mass-spectrometry technologies to profile Paracentrotus lividus tube feet differential proteome, comparing protein expression levels in its adhesive part (disc) versus the non-adhesive part (stem). This allowed us to identify 163 highly over-expressed disc proteins and propose the first molecular model of sea urchin reversible adhesion. The secreted adhesive proteome was also analyzed, whereby we found that 70% of its components fall within five protein groups, involved in adhesive exocytosis and protection against microbes. Our data also provides evidence that Nectin is not only highly expressed in tube feet discs but is a component of the adhesive itself, thus constituting the first report of a sea urchin tube foot adhesive protein. These results give us an unprecedented insight on the molecular mechanics underlying sea urchins reversible adhesion, opening new doors to develop new, wet-reliable, reversible, efficient, ecological biomimetic adhesives.