Shell matrix proteins of the clam, Mya truncata: Roles beyond shell formation through proteomic study

Jaison Arivalagan, Benjamin Marie, Victoria A. Sleight, Melody S. Clark, Sophie Berland, Arul Marie*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)


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 (α2 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.

Original languageEnglish
Pages (from-to)69-74
Number of pages6
JournalMarine Genomics
Publication statusPublished - 1 Jun 2016

Bibliographical note

Funding Information:
This research received funding from the European Union Seventh Framework Programme under grant agreement no. 605051 . G. Bolbach and L. Matheron (IBPS FR3631, UPMC, Paris) are kindly acknowledged for proteomics analysis and useful discussions.

Publisher Copyright:
© 2016 Elsevier B.V.


  • Biomineralization
  • Mya truncata
  • Shell matrix proteins


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