Recombinant Expression And Functional Analysis Of A New Type Of Shell Collagen From Mytilus Vulgaris
Keywords
Thick-Shelled Mussel, Shell Matrix Protein, Collagen Protein, Biomineralization
Abstract
Shell is a biological hard tissue with excellent mechanical properties, and shell matrix proteins are of great significance to the formation of shells. A new shell matrix protein similar to collagen was discovered in the shell of thick-shelled mussel (Mytilus coruscus), named collagen-like protein 2 (CLP-2). However, the structure and function of this protein and its impact on shell formation are still unclear. To this end, this study carried out sequence analysis of CLPª²2; further adopted codon optimization combined with a prokaryotic recombinant expression strategy to carry out recombinant expression of CLP-2; on this basis, the induction of calcium acid crystallization by recombinant CLP-2 was analyzed , crystallization rate inhibition and calcium carbonate binding ability. Sequence analysis of CLP-2 showed that the protein sequence contains a signal peptide and two Von Willebrand factor A (VWA) domains. CLP-2 does not yet have high homology proteins in the database, indicating that it is a relatively novel shell matrix protein. The obtained recombinant CLP-2 showed an obvious inducing effect on the in vitro crystallization of calcium carbonate. Scanning electron microscopy and Fourier transform infrared spectroscopy results showed that the recombinant CLP-2 could induce the morphology of calcium carbonate crystals to change from cubic to spherical, and It is further transformed into a dumbbell shape at high concentrations; at the same time, recombinant CLP-2 can promote the transformation of the crystal form of calcium carbonate crystals from calcite to aragonite; recombinant CLP-2 has a binding effect on calcium carbonate crystals in vitro; in addition, recombinant CLP -2 can significantly inhibit the crystallization speed of calcium carbonate crystals (P<0.01), and is concentration-dependent. The above results indicate that the CLP-2 protein of thick-shelled mussel shells plays an important role in the biomineralization process of shells, especially the aragonite-type myoprismatic layer. The above studies have laid the foundation for a deeper understanding of the formation mechanism of mussel shells and the impact of collagen proteins on the biomineralization process. For further information of this article and research, feel free to contact our team for asssitance. Original research was done by Jiang Yuting, Sun Qi, Liao Zhi, Zhang Xiaolin, Xu Huanzhi, Shen Wang, Fan Meihua
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