|Sea star tenacity mediated by a protein that fragments, then aggregates.
|Year of Publication
|Hennebert, E, Wattiez, R, Demeuldre, M, Ladurner, P, Hwang, DSoo, Waite, JH, Flammang, P
|Proc Natl Acad Sci U S A
|2014 Apr 29
|Adhesiveness, Animal Structures, Animals, Molecular Sequence Data, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, Proteins, Starfish
Sea stars adhere firmly but temporarily to various substrata as a result of underwater efficient adhesive secretions released by their tube feet. Previous studies showed that this material is mainly made up of proteins, which play a key role in its adhesiveness and cohesiveness. Recently, we solubilized the majority of these proteins and obtained 43 de novo-generated peptide sequences by tandem MS. Here, one of these sequences served to recover the full-length sequence of Sea star footprint protein 1 (Sfp1), by RT-PCR and tube foot transcriptome analysis. Sfp1, a large protein of 3,853 aa, is the second most abundant constituent of the secreted adhesive. By using MS and Western blot analyses, we showed that Sfp1 is translated from a single mRNA and then cleaved into four subunits linked together by disulphide bridges in tube foot adhesive cells. The four subunits display specific protein-, carbohydrate-, and metal-binding domains. Immunohistochemistry and immunocytochemistry located Sfp1 in granules stockpiled by one of the two types of adhesive cells responsible for the secretion of the adhesive material. We also demonstrated that Sfp1 makes up the structural scaffold of the adhesive footprint that remains on the substratum after tube foot detachment. Taken together, the results suggest that Sfp1 is a major structural protein involved in footprint cohesion and possibly in adhesive interactions with the tube foot surface. In recombinant form, it could be used for the design of novel sea star-inspired biomaterials.
|Proc. Natl. Acad. Sci. U.S.A.
|PubMed Central ID