Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell

Mollusca evolutionary success can be attributed partly to their efficiency to sustain and protect their soft body with an external biomineralized structure, the shell. Current knowledge of the protein set responsible for the formation of the shell microstructural polymorphism and unique properties r...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 109; no. 51; pp. 20986 - 20991
Main Authors Marie, Benjamin, Joubert, Caroline, Tayalé, Alexandre, Zanella-Cléon, Isabelle, Belliard, Corinne, Piquemal, David, Cochennec-Laureau, Nathalie, Marin, Frédéric, Gueguen, Yannick, Montagnani, Caroline
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 18.12.2012
National Acad Sciences
Subjects
Animal organs
Animals
Bioengineering
Biological Evolution
Biological Sciences
Biomaterials
Biomineralogy
Calcium Carbonate - chemistry
Datasets
Epithelium
Evolution
Evolution, Molecular
Evolutionary biology
Gene Expression Regulation
Genes
Immunohistochemistry
Life Sciences
Molecular Sequence Data
Mollusca - physiology
Mollusks
Nacre - metabolism
Oysters
Pearls
Pinctada - chemistry
Pinctada - physiology
Polymorphism
Protein Structure, Tertiary
Proteins
Proteome
Proteomics - methods
Shells
Transcription, Genetic
Transcriptome
mantle
evolution
mollusk shell matrix proteins
transcriptome
proteome
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Summary:Mollusca evolutionary success can be attributed partly to their efficiency to sustain and protect their soft body with an external biomineralized structure, the shell. Current knowledge of the protein set responsible for the formation of the shell microstructural polymorphism and unique properties remains largely patchy. In Pinctada margaritifera and Pinctada maxima, we identified 80 shell matrix proteins, among which 66 are entirely unique. This is the only description of the whole "biomineralization toolkit" of the matrices that at least in part, is thought to regulate the formation of the prismatic and nacreous shell layers in the pearl oysters. We unambiguously demonstrate that prisms and nacre are assembled from very different protein repertoires. This suggests that these layers do not derive from each other.
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1Present address: Unité Mixte de Recherche 7245 Centre National de la Recherche Scientifique Molécules de Communication et Adaptation des Micro-organismes, Muséum National d'Histoire Naturelle, 75005 Paris, France.
Edited* by Andrew H. Knoll, Harvard University, Cambridge, MA, and approved October 31, 2012 (received for review July 9, 2012)
Author contributions: B.M., N.C.-L., F.M., Y.G., and C.M. designed research; B.M., C.J., A.T., I.Z.-C., C.B., and C.M. performed research; C.J. and A.T. contributed new reagents/analytic tools; B.M., C.J., A.T., I.Z.-C., D.P., F.M., and C.M. analyzed data; and B.M., C.J., F.M., Y.G., and C.M. wrote the paper.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1210552109