@article {8124, title = {Deciphering shell proteome within different Baltic populations of mytilid mussels illustrates important local variability and potential consequences in the context of changing marine conditions}, journal = {Science of The Total Environment}, volume = {745}, year = {2020}, month = {Jan-11-2020}, pages = {140878}, issn = {00489697}, doi = {10.1016/j.scitotenv.2020.140878}, url = {https://linkinghub.elsevier.com/retrieve/pii/S0048969720344077}, author = {Arivalagan, Jaison and Marie, Benjamin and Chiappetta, Giovanni and Vinh, Jo{\"e}lle and Gallet, Xavier and Lebon, Matthieu and M{\textquoteright}Zoudi, Saloua and Dubois, Philippe and Berland, Sophie and Marie, Arul} } @article {4728, title = {Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa}, journal = {Journal of The Royal Society Interface}, volume = {14}, year = {2017}, 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 {\textquoteleft}calcifying matrix{\textquoteright} 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).

}, issn = {1742-5689}, doi = {10.1098/rsif.2016.0846}, url = {http://rsif.royalsocietypublishing.org/content/14/126/20160846}, author = {Marie, Benjamin and Arivalagan, Jaison and Math{\'e}ron, Lucr{\`e}ce and Bolbach, G{\'e}rard and Berland, Sophie and Marie, Arul and Marin, Fr{\'e}d{\'e}ric} } @article {4526, title = {First proteomic analyses of the dorsal and ventral parts of the Sepia officinalis cuttlebone.}, journal = {J Proteomics}, volume = {150}, year = {2017}, month = {2016 Aug 26}, pages = {63-73}, abstract = {

Protein compounds constituting mollusk shells are known for their major roles in the biomineralization processes. These last years, a great diversity of shell proteins have been described in bivalves and gastropods allowing a better understanding of the calcification control by organic compounds and given promising applications in biotechnology. Here, we analyzed for the first time the organic matrix of the aragonitic Sepia officinalis shell, with an emphasis on protein composition of two different structures: the dorsal shield and the chambered part. Our results highlight an organic matrix mainly composed of polysaccharide, glycoprotein and protein compounds as previously described in other mollusk shells, with quantitative and qualitative differences between the dorsal shield and the chamber part. Proteomic analysis resulted in identification of only a few protein compounds underlining the lack of reference databases for Sepiidae. However, most of them contain domains previously characterized in matrix proteins of aragonitic shell-builder mollusks, suggesting ancient and conserved mechanisms of the aragonite biomineralization processes within mollusks.

BIOLOGICAL SIGNIFICANCE: The cuttlefish{\textquoteright}s inner shell, better known under the name "cuttlebone", is a complex mineral structure unique in mollusks and involved in tissue support and buoyancy regulation. Although it combines useful properties as high compressive strength, high porosity and high permeability, knowledge about organic compounds involved in its building remains limited. Moreover, several cuttlebone organic matrix studies reported data very different from each other or from other mollusk shells. Thus, this study provides 1) an overview of the organization of the main mineral structures found in the S. officinalis shell, 2) a reliable baseline about its organic composition, and 3) a first descriptive proteomic approach of organic matrices found in the two main parts of this shell. These data will contribute to the general knowledge about mollusk biomineralization as well as in the identification of protein compounds involved in the Sepiidae shell calcification.

}, issn = {1876-7737}, doi = {10.1016/j.jprot.2016.08.015}, author = {Le Pabic, Charles and Marie, Arul and Marie, Benjamin and Percot, Aline and Laure Bonnaud-Ponticelli and Pascal Jean Lopez and Gilles Luquet} } @article {4575, title = {Insights from the shell proteome: biomineralization to adaptation.}, journal = {Mol Biol Evol}, year = {2016}, month = {2016 Oct 15}, abstract = {

Bivalves have evolved a range of complex shell forming mechanisms that are reflected by their incredible diversity in shell mineralogy and microstructures. A suite of proteins exported to the shell matrix space plays a significant role in controlling these features, in addition to underpinning some of the physical properties of the shell itself. Although, there is a general consensus that a minimum basic protein tool kit is required for shell construction, to date, this remains undefined. In this study the shell matrix proteins (SMPs) of four highly divergent bivalves (The Pacific oyster, Crassostrea gigas; the blue mussel, Mytilus edulis; the clam, Mya truncata and the king scallop, Pecten maximus) were analyzed in an identical fashion using proteomics pipeline. This enabled us to identify the critical elements of a "basic tool kit" for calcification processes, which were conserved across the taxa irrespective of the shell morphology and arrangement of the crystal surfaces. In addition, protein domains controlling the crystal layers specific to aragonite and calcite were also identified. Intriguingly, a significant number of the identified SMPs contained domains related to immune functions. These were often are unique to each species implying their involvement not only in immunity, but also environmental adaptation. This suggests that the SMPs are selectively exported in a complex mix to endow the shell with both mechanical protection and biochemical defense.

}, issn = {1537-1719}, doi = {10.1093/molbev/msw219}, author = {Arivalagan, Jaison and Yarra Teja and Marie, Benjamin and Sleight, Victoria A and Duvernois-Berthet, Evelyne and Clark, Melody S and Marie, Arul and Berland, Sophie} } @article {4270, title = {Shell matrix proteins of the clam, Mya truncata: Roles beyond shell formation through proteomic study}, journal = {Marine Genomics}, volume = {27}, year = {2016}, month = {06/2016}, pages = {69-74}, abstract = {

Abstract Mya truncata, a soft shell clam, is presented as a new model to study biomineralization through a proteomics approach. In this study, the shell and mantle tissue were analysed in order to retrieve knowledge about the secretion of shell matrix proteins (SMPs). Out of 67 and 127 shell and mantle proteins respectively, 16 were found in both shell and mantle. Bioinformatic analysis of \{SMP\} sequences for domain prediction revealed the presence of several new domains such as fucolectin tachylectin-4 pentraxin-1 (FTP), scavenger receptor, alpha-2-macroglobulin ({\OE}{\textpm}2 M), lipocalin and myosin tail along with previously reported \{SMP\} domains such as chitinase, carbonic anhydrase, tyrosinase, sushi, and chitin binding. Interestingly, these newly predicted domains are attributed with molecular functions other than biomineralization. These findings suggest that shells may not only act as protective armour from predatory action, but could also actively be related to other functions such as immunity. In this context, the roles of \{SMPs\} in biomineralization need to be looked in a new perspective.

}, keywords = {biomineralization}, issn = {1874-7787}, doi = {http://dx.doi.org/10.1016/j.margen.2016.03.005}, url = {http://www.sciencedirect.com/science/article/pii/S1874778716300186}, author = {Arivalagan, Jaison and Marie, Benjamin and Victoria A. Sleight and Melody S. Clark and Berland, Sophie and Marie, Arul} } @inbook {4068, title = {Unveiling the evolution of bivalve nacre proteins by shell proteomics of Unionoidae. }, booktitle = {Biomineralization: from fundamentals to biomaterials \& environmental issues}, volume = {672}, year = {2015}, pages = {pp.158-167}, edition = {Key Engineering Materials, 978-3-03835-591-5 Trans Tech Publications Ltd}, chapter = {2}, author = {Marie, Benjamin and Arivalagan, Jaison and Dubost, Lionel and Berland, Sophie and Marie, Arul and Marin, Fr{\'e}d{\'e}ric} }