Proteomics

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Proteomic analysis of the shell organic matrix of Spondylus Gaederopus


ABSTRACT: This work reports a comprehensive and integrated microstructural, biochemical and proteomics study on the shell matrix of Spondylus gaederopus, the Mediterranean thorny oyster. We investigate the skeletal matrix proteins which are involved in biomineralization and compare the identified Spondylus sequences with other shell proteins, that are publicly available in databases. Using high-resolution liquid chromatography tandem mass spectrometry (LC-MS/MS) we characterized several shell protein fractions, isolated by different bleaching treatments. We identified six shell proteins, which also displayed features and domains typically found in biomineralized tissues, including the prevalence of intrinsically disordered regions. However, many reconstructed peptide sequences (de novo) could not be matched to any known shell proteins and we suggest that these probably represent lineage-specific sequences. The proteomic data implies that Spondylus may have evolved a distinct molecular toolkit for biomineralization. Using high-resolution liquid chromatography tandem mass spectrometry (LC-MS/MS) we characterized several shell protein fractions, isolated by different bleaching treatments. Six shell proteins were identified, which displayed features and domains typically found in biomineralized tissues, including the prevalence of intrinsically disordered regions. However, most of the reconstructed peptide sequences (de novo) could not be matched to any known shell proteins and probably represent lineage-specific sequences.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Spondylus Gaederopus

TISSUE(S): Exoskeleton

SUBMITTER: Jorune Sakalauskaite  

LAB HEAD: Frédéric Marin

PROVIDER: PXD016760 | Pride | 2020-03-31

REPOSITORIES: Pride

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Publications

The shell matrix of the european thorny oyster, Spondylus gaederopus: microstructural and molecular characterization.

Sakalauskaite Jorune J   Plasseraud Laurent L   Thomas Jérôme J   Albéric Marie M   Thoury Mathieu M   Perrin Jonathan J   Jamme Frédéric F   Broussard Cédric C   Demarchi Beatrice B   Marin Frédéric F  

Journal of structural biology 20200324 1


Molluscs, the largest marine phylum, display extraordinary shell diversity and sophisticated biomineral architectures. However, mineral-associated biomolecules involved in biomineralization are still poorly characterised. We report the first comprehensive structural and biomolecular study of Spondylus gaederopus, a pectinoid bivalve with a peculiar shell texture. Used since prehistoric times, this is the best-known shell of Europe's cultural heritage. We find that Spondylus microstructure is ver  ...[more]

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