Shell acidic matrix proteins are widely considered to be essential for shell formation given their low affinity and high loading for calcium ion. In the present study, a novel matrix protein, hic12, was isolated from the mantle of Hyriopsis cumingii. High expression in tissue and positive signals with in situ hybridization were detected in the mantle center and mantle pallium, indicating that hic12 mainly participated in the biomineralization of the shell nacreous layer. The expression pattern of hic12 in the pearl sac during early pearl formation indicated that it was involved in pearl biomineralization. Moreover, the recombinant protein, rGST-Hic12, was successfully expressed and purified. The addition of rGST-Hic12 could accelerate the calcium carbonate deposition rate, change the morphology of crystals, and promote the conversion of calcite to vaterite. These results may provide new insights into the molecular mechanisms of aragonite mollusk shell formation.
Keywords: Biomineralization; Hyriopsis cumingii; Matrix protein; Nacreous layer; Pearl; Vaterite.
Copyright © 2022. Published by Elsevier Inc.