Ps19, a novel chitin binding protein from Pteria sterna capable to mineralize aragonite plates in vitro

Arroyo-Loranca, Raquel G.; Hernández-Saavedra, Norma Y.; Hernández‐Adame, Luis; Rivera-Pérez, Crisalejandra

doi:10.1371/journal.pone.0230431

Cited by 14 publications

(18 citation statements)

References 56 publications

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“…Chitin synthases have also been found in transcriptome data of P. penguin reported by Li et al [ 2 ]. Additionally, numerous examples of chitin-binding proteins that show important roles on biomineralization involved in nacreous layer formation such as Pif-like [ 17 , 18 ], pearlin/N16 family [ 19 ], Hichin [ 20 ] and PS19 [ 21 ], etc., have been reported. Taken together with PPL4 activity with chitin oligomer, PPL4 may participate in the biomineralization process of P. penguin nacre and the D-shell formation from an early stage as chitin-binding proteins and calcium carbonate crystallization regulators.…”

Section: Discussionmentioning

confidence: 99%

Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins

Ogawa

Sato

Naganuma

et al. 2021

IJMS

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Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation.

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Section: Discussionmentioning

confidence: 99%

Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins

Ogawa

Sato

Naganuma

et al. 2021

IJMS

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“…The powdered matrices (20 g) were suspended in 100 mL cold acetic acid (4 °C, 10% v/v) and incubated 24 h with continuous stirring. Acetic acid-soluble matrix fractions (ASM) and acetic acid-insoluble matrix fractions (AIM) were separated by centrifugation at 13,000 × g for 20 min 74 . The AIM was rinsed with distilled water and lyophilized.…”

Section: Methodsmentioning

confidence: 99%

“…Quantification of pearlin present in the AIM was performed by pixel densitometry as described by Arroyo-Loranca 74 . Briefly, a standard curve was performed using ovalbumin protein (0.25-7.0 µg/µL) and the linear equation obtained was used for the pearlin protein quantification, y = 10138x-4163.7 ( Supplementary Fig.…”

Section: Protein Quantificationmentioning

confidence: 99%

“…Pearlin purification by preparative SDS-PAGE. The identified pearlin from the AIM was isolated using a preparative polyacrylamide gel electrophoresis according to the Mini-Prep Cell Manual (Bio-Rad, model 491 Prep Cell), using 20 mg of lyophilized AIM according to Arroyo-Loranca 74 . Proteins containing the pearlin protein were pooled, concentrated using an Amicon-Ultra filter (10,000 MW cut-off) and desalted using 30 mM Tris-HCl buffer pH 8.8.…”

Section: Immunodetection Of Pearlin By Western Blot Polyclonal Antibmentioning

confidence: 99%

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A shell matrix protein of Pinctada mazatlanica produces nacre platelets in vitro

Rivera-Pérez

Flores-Sánchez

Areyano

et al. 2020

Sci Rep

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Nacre is the main component of the pearl oyster shells and it is synthesized by specialized soluble and insoluble shell matrix proteins. Insoluble proteins from the decalcification of the shell are the less studied proteins due to the technical problems to isolate them from the organic matrix. In this study, an insoluble shell matrix protein from Pinctada mazatlanica, pearlin (Pmaz-pearlin), was successfully cloned from the mantle tissue, and the native protein isolated from the shell was functionally characterized. The full coding sequence of Pmaz-pearlin mRNA consists of 423 base pairs, which encode to a 16.3 kDa pearlin. Analysis of the deduced amino acid sequence revealed that Pmaz-pearlin contained four acidic regions, an NG repeat domain, and Cys conserved residues, the latter potentially forms four disulfide bridges which might stabilize the protein structure. The isolated protein from the shell is a glycoprotein of ~ 16.74 kDa which can produce aragonite and calcite crystals in vitro. Our results show that Pmaz-pearlin is a well-conserved protein involved in nacre layer growth, which produces calcite crystals in the presence of CaCl2, aragonite crystal polymorphs with a hexagonal structure in the presence of MgCl2, and needle-like crystal structure polymorphs in the presence of CaCO3 The identity of the crystals was confirmed using RAMAN analyses.

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“…However, many proteins encoding the chitin-binding domain in the highly expressed genes of the outer fold are enriched in the chitin catabolic process, N-acetyl-beta-D-galactosaminidase activity and other biological processes. Proteins with chitin-binding domains play an important role in the shell biological mineralisation and shell structural composition and can bind with calcium and chitin to participate in shell growth [44][45][46][47][48][49] . As an important component of the shell skeleton, chitin acts as a coordinating switch between the forming shell and the cells 50 and plays an important role in shell biological mineralisation 51,52 .…”

Section: The Three Folds Of Mantle Edge Are Functionally Differentiat...mentioning

confidence: 99%

A Chitin-Binding Protein Ultra-highly expressed in the Outer Fold of Mantle is Related to Shell Colour in Pacific Oyster Crassostrea gigas

Oliver¹

2022

Preprint

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Molluscs constitute the second largest Phylum of animals in the world, and shell colour and stripes are one of their most important phenotypic characteristics. Studies on the mechanism of shell pigmentation help understand the evolutionary and ecological importance of shell colour and serve as the basis for shell colour breeding. In this study, a matched-pair design was used in comparing the black- and white-striped mantles of the same oyster. The result showed that the stripes of shell surface are corresponding to the stripes of the mantle edge. Transcriptomic analysis identified a gene (named as Crassostrea gigas chitin-binding protein, CgCBP) highly expressed in the black mantles. Three folds were found on the mantle edge of oyster, but only the outer fold has the same colour as the shell. Transcriptomic comparison indicated that the three folds of the mantle edge are functionally differentiated, and the CgCBP gene is ultra-highly expressed only in the outer fold. We obtained new black and white shell periostraca from the shell notching experiment and found their structural differences by scanning electron microscope. Chitin was successfully extracted and identified from the shell periostraca. Proteomic analysis revealed differences in protein composition between the two shell periostraca. Particularly, the black shell periostraca have more proteins related to melanin biosynthesis and chitin binding compared with the white ones, and melanin particles were observed in the black mantle edge using transmission electron microscope. Magnetic bead binding and Western blot experiments showed that the CgCBP protein can specifically bind to chitin and in vivo RNAi screening indicated that CgCBP knockdown can change the structure of the shell periostracum and reduce its pigmentation. All these results suggest that the outer fold of the mantle may have more important roles in shell pigmentation, shell periostracum structure is functionally correlated with shell pigmentation, and the CgCBP gene ultra-highly expressed in the outer fold may influence shell pigmentation by affecting its periostracum structure.

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Ps19, a novel chitin binding protein from Pteria sterna capable to mineralize aragonite plates in vitro

Cited by 14 publications

References 56 publications

Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins

Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins

A shell matrix protein of Pinctada mazatlanica produces nacre platelets in vitro

A Chitin-Binding Protein Ultra-highly expressed in the Outer Fold of Mantle is Related to Shell Colour in Pacific Oyster Crassostrea gigas

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