title: Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa.
abstract: 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, glycoproteins and polysaccharides that is assembled and occluded within the mineral phase during the calcification process. Better molecular-level characterization of the substances that regulate nacre formation is still required. Notable advances in expressed tag sequencing of freshwater mussels, such as Elliptio complanata and Villosa lienosa, provide a pre-requisite to further characterize bivalve nacre proteins by a proteomic approach. In this study, we have identified a total of 48 different proteins from the insoluble matrices of the nacre, 31 of which are common to both E. complanata and V. lienosa A few of these proteins, such as PIF, MSI60, CA, shematrin-like, Kunitz-like, LamG, chitin-binding-containing proteins, together with A-, D-, G-, M- and Q-rich proteins, appear to be analogues, if not true homologues, of proteins previously described from the pearl oyster or the edible mussel nacre matrices, thus forming a remarkable list of deeply conserved nacre proteins. This work constitutes a comprehensive nacre proteomic study of non-pteriomorphid bivalves that has enabled us to describe the molecular basis of a deeply conserved biomineralization toolkit among nacreous shell-bearing bivalves, with regard to proteins associated with other shell microstructures, with those of other mollusc classes (gastropods, cephalopods) and, finally, with other lophotrochozoans (brachiopods).
authors.affiliation: UMR 7245 CNRS/MNHN Molécules de Communications et Adaptations des Micro-organismes, Muséum National d'Histoire Naturelle, Sorbonne Universités, Paris, France bmarie@mnhn.fr.
authors.forename: Benjamin
authors.identifier: 0000-0001-9880-5541
authors.initials: B
authors.lastname: Marie
authors.affiliation: UMR 7245 CNRS/MNHN Molécules de Communications et Adaptations des Micro-organismes, Muséum National d'Histoire Naturelle, Sorbonne Universités, Paris, France.
authors.forename: Jaison
authors.initials: J
authors.lastname: Arivalagan
authors.affiliation: UMR 7203 CNRS/UPMC/ENS/INSERM Laboratoire des Biomolécules, Institut de Biologie Paris Seine, Université Pierre et Marie Curie, Sorbonne Universités, Paris, France.
authors.forename: Lucrèce
authors.initials: L
authors.lastname: Mathéron
authors.affiliation: UMR 7203 CNRS/UPMC/ENS/INSERM Laboratoire des Biomolécules, Institut de Biologie Paris Seine, Université Pierre et Marie Curie, Sorbonne Universités, Paris, France.
authors.forename: Gérard
authors.initials: G
authors.lastname: Bolbach
authors.affiliation: UMR 7208 CNRS/MNHN/UPMC/IRD Biologie des Organismes Aquatiques et Ecosystèmes, Muséum National d'Histoire Naturelle, Sorbonne Universités, Paris, France.
authors.forename: Sophie
authors.initials: S
authors.lastname: Berland
authors.affiliation: UMR 7245 CNRS/MNHN Molécules de Communications et Adaptations des Micro-organismes, Muséum National d'Histoire Naturelle, Sorbonne Universités, Paris, France.
authors.forename: Arul
authors.initials: A
authors.lastname: Marie
authors.affiliation: UMR 6282 CNRS/uB Biogéosciences, Université de Bourgogne Franche-Comté (UB-FC), Dijon, France.
authors.forename: Frédéric
authors.initials: F
authors.lastname: Marin
mesh_terms: D060105:Animal Shells / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D002113:Calcification, Physiologic / Q000502:physiology*; D019143:Evolution, Molecular; D016326:Extracellular Matrix Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D060734:Nacre / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040901:Proteomics; D049876:Unionidae / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism
chemical_list: D016326:Extracellular Matrix Proteins; D060734:Nacre
keywords: biomineralization; bivalve; calcium carbonate; organic matrix proteins; proteomics; shell nacre