0000000001079134
AUTHOR
Arul Marie
Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa.
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…
Nacre evolution: a proteomic approach.
AbstractFrom an evolutionary viewpoint, the molluscan nacre constitutes a fascinating object. This microstructure appeared early, in the Lower Cambrian period, about 530 million years ago, and since then, has been kept unchanged until today. Nacre is restricted to the conchiferan mollusks, where it occurs in t least three main classes, bivalves, gastropods and cephalopods. The aim of the present study is to investigate whether all nacres are built from the same “macromolecular tools”, proteins of the nacre matrix. To this end, we studied three new nacre models, the freshwater bivalve Unio pictorum, the cephalopod Nautilus macromphalus, and the gastropod Haliotis asinina, to which we applied…
Proteomics of CaCO3 biomineral-associated proteins: how to properly address their analysis.
8 pages; International audience; In a recent editorial (Proc. Natl. Acad. Sci., 2013 110, E2144-E2146) and elsewhere, questions have been raised regarding the experimental practices in relation to the proteomic analysis of organic matrices associated to the biomineralized CaCO3 skeletons of metazoans such as molluscan shells and coral skeletons. Indeed, although the use of new high sensitivity MS technology potentially allows to identify a greater number of proteins, it is also equally (or even more) sensitive to contamination of residual proteins from soft tissues, which are in close contact with the biomineral. Based on our own past and present experimental know-how-observations that are …
Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus
Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemag…
Characterization of the teeth skeletal matrix from Arbacia lixula.
15 pages; International audience
Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shell.
Abstract Background The formation of the molluscan shell 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, most of its protein components remain uncharacterised. Results Recent expressed sequence tag (EST) investigations of the mantle tissue from the tropical abalone (Haliotis asinina) provide an opportunity to further characterise the proteins …
Supplementary figures from Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa
figures S1-S3
Evolution of nacre: biochemistry and proteomics of the shell organic matrix of the cephalopod Nautilus macromphalus.
12 pages; International audience; In mollusks, one of the most widely studied shell textures is nacre, the lustrous aragonitic layer that constitutes the internal components of the shells of several bivalves, a few gastropods, and one cephalopod: the nautilus. Nacre contains a minor organic fraction, which displays a wide range of functions in relation to the biomineralization process. Here, we have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus. The acid-soluble matrix contains a mixture of polydisperse and discrete proteins and glycoproteins, which interact with the formation of calcite crystals. In addition, a few bind calcium ions. Furthermore, we h…
Characterization of the Teeth Skeletal Matrix from <i>Arbacia lixula</i>
The teeth of sea urchins are highly complex composite structures, composed predominantly of high magnesium calcite, and of a minor heterogeneous assemblage of organic macromolecules that are occluded within the mineral. The organic matrix fulfils important functions in mineralization, in addition to giving the mineral phase peculiar mechanical properties, different from that of purely inorganic calcite. Nevertheless, the composition and function of individual components of the organic matrix still remains largely unknown. Up to now, the detailed protein repertoire of teeth from a single sea urchin species (Strongylocentrotus purpuratus, order Camarodonta) was investigated. In this study, we…
Unveiling the evolution of bivalve nacre proteins by shell proteomics of Unionoidae.
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 pr…
Shell proteome of rhynchonelliform brachiopods.
7 pages; International audience; Brachiopods are a phylum of marine invertebrates that have an external bivalved shell to protect their living tissues. With few exceptions, this biomineralized structure is composed of calcite, mixed together with a minor organic fraction, comprising secreted proteins that become occluded in the shell structure, once formed. This organic matrix is thought to display several functions, in particular, to control mineral deposition and to regulate crystallite shapes. Thus, identifying the primary structure of matrix proteins is a prerequisite for generating bioinspired materials with tailored properties. In this study, we employed a proteomic approach to identi…
Supplementary table from Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa
Table S1