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Ps19, a novel chitin binding protein from Pteria sterna capable to mineralize aragonite plates in vitro
RAQUEL GABRIELA ARROYO LORANCA
NORMA YOLANDA HERNANDEZ SAAVEDRA
LUIS HERNANDEZ ADAME
Crisalejandra Rivera Pérez
Acceso Abierto
Atribución-NoComercial-SinDerivadas
DOI: 10.1371/journal.pone.0230431
ISSN: 1932-6203
URL: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0230431
Pteria sterna, Mollusk shell
"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."
Public Library of Science
2020
Artículo
PLoS ONE
Inglés
Arroyo-Loranca RG, Hernandez-Saavedra NY, Hernandez-Adame L, Rivera-Perez C (2020) Ps19, a novel chitin binding protein from Pteria sterna capable to mineralize aragonite plates in vitro. PLoS ONE 15(3): e0230431. https://doi.org/ 10.1371/journal.pone.0230431
FISIOLOGÍA ANIMAL
Versión publicada
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