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Ps19, a novel chitin binding protein from Pteria sterna capable to mineralize aragonite plates in vitro.
- Source :
-
PloS one [PLoS One] 2020 Mar 19; Vol. 15 (3), pp. e0230431. Date of Electronic Publication: 2020 Mar 19 (Print Publication: 2020). - Publication Year :
- 2020
-
Abstract
- Mollusk shell is composed of two CaCO3 polymorphs (calcite and aragonite) and an organic matrix that consists of acetic acid- or ethylenediaminetetraacetic acid (EDTA)-soluble and insoluble proteins and other biomolecules (polysaccharides, β-chitin). However, the shell matrix proteins involved in nacre formation are not fully known. Thus, the aim of this study was to identify and characterize a novel protein from the acetic acid-insoluble fraction from the shell of Pteria sterna, named in this study as Ps19, to have a better understanding of the biomineralization process. Ps19 biochemical characterization showed that it is a glycoprotein that exhibits calcium- and chitin-binding capabilities. Additionally, it is capable of inducing aragonite plate crystallization in vitro. Ps19 partial peptide sequence showed similarity with other known shell matrix proteins, but it displayed similarity with proteins from Crassostrea gigas, Mizuhopecten yessoensis, Biomphalaria glabrata, Alpysia californica, Lottia gigantea and Elysia chlorotica. The results obtained indicated that Ps19 might play an important role in nacre growth of mollusk shells.<br />Competing Interests: The authors have declared that no competing interests exist.
- Subjects :
- Amino Acid Sequence
Animals
Carrier Proteins chemistry
Carrier Proteins isolation & purification
Crystallization
Peptides chemistry
Peptides metabolism
Salts
Solubility
Spectrum Analysis, Raman
Calcification, Physiologic
Calcium Carbonate metabolism
Carrier Proteins metabolism
Chitin metabolism
Pinctada metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 15
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 32191756
- Full Text :
- https://doi.org/10.1371/journal.pone.0230431