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

Arivalagan, Jaison; Marie, Benjamin; Sleight, Victoria A. ORCID:; Clark, Melody S. ORCID:; Berland, Sophie; Marie, Arul. 2016 Shell matrix proteins of the clam, Mya truncata: Roles beyond shell formation through proteomic study. Marine Genomics, 27. 69-74.

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This article has been accepted for publication and will appear in a revised form in Marine Genomics, published by Elsevier. Copyright Elsevier.
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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.

Item Type: Publication - Article
Digital Object Identifier (DOI):
Programmes: BAS Programmes > BAS Programmes 2015 > Biodiversity, Evolution and Adaptation
ISSN: 18747787
Additional Keywords: Mya truncate, shell matrix proteins, biomineralization
Date made live: 12 Apr 2016 08:23 +0 (UTC)

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