6533b870fe1ef96bd12cfd62

RESEARCH PRODUCT

Unveiling the evolution of bivalve nacre proteins by shell proteomics of Unionoidae.

subject

description

The formation of the molluscan shell nacre is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell forming tissue, the mantle. This so called “calcifying matrix” is a complex mixture of proteins and glycoproteins that is assembled and occluded within the mineral phase during the calcification process. While the importance of the calcifying matrix to shell formation has long been appreciated, the molecular basis that dictates nacre formation remains largely uncharacterized.Recent expressed sequence tag (EST) investigations of the freshwater mussels (Elliptio complanata and Villosa leinosa) provide an opportunity to further characterize the proteins in the bivalve shell by a proteomic approach. In this study, we have identified a total of 15 proteins from their nacre insoluble matrices. Few of these proteins, such as Pif, MSI60, Nacrein-like, Shematrin, Kunitz-like containing, Papilin-like, LamG containing, Chitin-binding containing, M-rich and Q-rich proteins, appear to be analogs, if not true homologs, of proteins previously described from the pearl oyster or the edible mussel nacre matrices. This work constitutes a comprehensive EST-based nacre proteomic study of non-pteriomorphid bivalves that concretely gives us the opportunity to describe the molecular basis of deeply conserved nacre biomineralization toolkit within nacreous shell bearing bivalves.