Proteomic and profile analysis of the proteins laced with aragonite and vaterite in the freshwater mussel Hyriopsis cumingii shell biominerals.

Abstract : Hyriopsis cumingii (Lea, Unionidae), a freshwater bivalve species widely distributed in China and commercially exploited for freshwater pearl production, was chosen as the reference model to investigate the protein signature in the organic scaffold matching calcium carbonate crystallization mode. This study takes advantage of different calcium carbonate habits production by the organism: aragonite in shell and pearl and vaterite in alternative pearl formation. Amino acid global composition and proteomics analysis have been undertaken to study the amino acid imbalance with respect to biominerals and microstructures. Forty peptides sequences were obtained by proteomics, of which ten are shared by all the different samples, nine are laced with aragonite; another nine with vaterite and twelve are related to pearls. Bioinformatics analysis allowed the peptides to be matched to the deduced protein sequences from EST databases and allowed functional assignment (e.g. scaffolding, strain strength, chitin binding or carbonic anhydrase function) to the proteins found in the different materials. Such panel of motifs tailored in vaterite and aragonite habits produced in a freshwater mollusk gives food for thought about organic control of the biomineralization processes.
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Article dans une revue
Protein and Peptide Letters, Bentham Science Publishers, 2013, 20 (10), pp.1170-80
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http://hal.univ-grenoble-alpes.fr/hal-01322412
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Soumis le : vendredi 27 mai 2016 - 10:38:52
Dernière modification le : vendredi 31 août 2018 - 09:18:24

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  • HAL Id : hal-01322412, version 1
  • PUBMED : 23409939

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Sophie Berland, Yufei Ma, Arul Marie, Jean-Pierre Andrieu, Laurent Bedouet, et al.. Proteomic and profile analysis of the proteins laced with aragonite and vaterite in the freshwater mussel Hyriopsis cumingii shell biominerals.. Protein and Peptide Letters, Bentham Science Publishers, 2013, 20 (10), pp.1170-80. 〈hal-01322412〉

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