Caspartin and calprismin, two proteins of the shell calcitic prisms of the mediterranean fan mussel Pinna nobilis

doi:10.1074/jbc.M506526200

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Papers In Press, published online ahead of print July 1, 2005
J. Biol. Chem, 10.1074/jbc.M506526200
Submitted on June 15, 2005
Revised on June 30, 2005
Accepted on July 1, 2005

Caspartin and calprismin, two proteins of the shell calcitic prisms of the mediterranean fan mussel Pinna nobilis

Frédéric Marin, Reinout Amons, Nathalie Guichard, Martin Stitger, Arnaud Hecker, Gilles Luquet, Pierre Layrolle, Gérard Alcaraz, Christophe Riondet, and Peter Westbroek

UMR CNRS 5561 Biogéosciences, Université de Bourgogne, DIJON 21000

Corresponding Author: frederic.marin{at}u-bourgogne.fr

We used the combination of preparative electrophoresis and immunological detection to isolate two new proteins from the shell calcitic prisms of Pinna nobilis, the Mediterranean fan mussel. The amino acid composition of these proteins was determined. Both proteins are soluble, intra-crystalline and acidic. The 38-kDa protein is glycosylated; the 17-kDa one is not. Ala, Asx, Thr and Pro represent the dominant residues of the 38-kDa protein, named calprismin. A 61 N-terminal amino acid sequence was obtained from calprismin. This sequence, which comprises a pattern of 4 cysteine residues, is not related to any known protein. The second protein, named caspartin, exhibits an unusual amino acid composition since Asx constitutes by far the main amino acid residue. Preliminary sequencing surprisingly suggests that the first N-terminal 75 residues are all Asp. Caspartin self-aggregates spontaneously into multimers. In vitro tests show that it inhibits the precipitation of calcium carbonate. Furthermore, it strongly interferes with the growth of calcite crystals. A polyclonal antiserum raised against caspartin was used to localize this protein in the shell by immunogold. The immunolocalization demonstrates that caspartin is distributed within the prisms and makes a continuous film at the interface between the prisms and the surrounding insoluble sheets. Our finding emphasizes the prominent role of aspartic acid-rich proteins for the building of calcitic prisms among mollusks.

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