Microstructure and in-depth proteomic analysis of Perna viridis shell

Liao, Zhi; Jiang, Yuting; Sun, Qi; Fan, Meihua; Wang, Jianxin; Liang, Haiying

doi:10.1371/journal.pone.0219699

Cited by 31 publications

(28 citation statements)

References 94 publications

(142 reference statements)

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“…Ps19 showed a high proportion of these residues (17%); therefore it may have been an acidic protein and its isolation was difficult, having low yield (18%) extraction but high purity (85%). Acetic acid-insoluble proteins from other species have been extracted and an attempt to describe and characterize them all has been done, and although some have been described, many still remain to be characterized; their role in shell biomineralization is still unknown [12,28,45].…”

Section: Discussionmentioning

confidence: 99%

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

Arroyo-Loranca¹,

Hernández-Saavedra²,

Hernández‐Adame³

et al. 2020

PLoS ONE

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Mollusk shell is composed of two CaCO 3 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.

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Section: Discussionmentioning

confidence: 99%

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

Arroyo-Loranca¹,

Hernández-Saavedra²,

Hernández‐Adame³

et al. 2020

PLoS ONE

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“…The results showed substantial signals of the two proteins and the overlapping pattern of WLP and actin on the shell surface of the myostracum layer (Fig 11). The identification of actin, and other cytoskeletal proteins in various mollusc shells has been controversial [8,23,26,46]. We cannot exclude the possibility that actin may participate in biomineralization by interacting with actin-binding proteins (such as WLP in this study) and forming a framework during shell formation.…”

Section: Plos Onementioning

confidence: 82%

“…PDCPs have been previously identified in various mollusc shells, including WLP, PDZ/ZM, and PDZ/LIM domain-containing proteins [8,[23][24][25][26]. BLAST results revealed the high homology of WLP with PDCPs from other bivalves.…”

Section: Discussionmentioning

confidence: 99%

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Molecular characterization of a whirlin-like protein with biomineralization-related functions from the shell of Mytilus coruscus

et al. 2020

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Mollusc shells are produced from calcified skeletons and have excellent mechanical properties. Shell matrix proteins (SMPs) have important functions in shell formation. A 16.6 kDa whirlin-like protein (WLP) with a PDZ domain was identified in the shell of Mytilus coruscus as a novel SMP. In this study, the expression, function, and location of WLP were analysed. The WLP gene was highly expressed and specifically located in the adductor muscle and mantle. The expression of recombinant WLP (rWLP) was associated with morphological change, polymorphic change, binding ability, and crystallization rate inhibition of the calcium carbonate crystals in vitro. In addition, an anti-rWLP antibody was prepared, and the results from immunohistochemistry and immunofluorescence analyses revealed the specific location of the WLP in the mantle, adductor muscle, and myostracum layer of the shell, suggesting multiple functions for WLP in biomineralization, muscle-shell attachment, and muscle attraction. Furthermore, results from a pull-down analysis revealed 10 protein partners of WLP in the shell matrices and a possible network of interacting WLPs in the shell. In addition, in this study, one of the WLP partners, actin, was confirmed to have the ability to bind WLP. These results expand the understanding of the functions of PDZ-domain-containing proteins in biomineralization and provide clues for determining the mechanisms of myostracum formation and muscle-shell attachment. OPEN ACCESS Citation: Jiang Y, Sun Q, Fan M, Zhang X, Shen W, Xu H, et al. (2020) Molecular characterization of a whirlin-like protein with biomineralization-related functions from the shell of Mytilus coruscus. PLoS ONE 15(4): e0231414. https://doi.org/10.

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“…In addition, the ZM domain is a short motif (26 amino acids) first found in the alpha-actinin-binding protein ZASP (Z-band alternatively spliced PDZ-motif protein), and it is frequently found in association with PDZ domains in a number of cytoskeletal and muscle proteins ( Faulkner et al, 1999 ; Klaavuniemi et al, 2004 ). PDZ-domain-containing proteins (PDCPs) have been identified from the shells of various Mollusca genera, including Mytilus ( Gao et al, 2015 ; Liao et al, 2015 ), Ostrea ( Zhang et al, 2012 ), Pinctada ( Sarah et al, 2015 ), and Perna ( Liao et al, 2019 ). The roles of PDCPs in shell formation remain a mystery.…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization of a Novel Shell Matrix Protein With PDZ Domain From Mytilus coruscus

et al. 2020

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Mollusk shells are products of biomineralization and possess excellent mechanical properties, and shell matrix proteins (SMPs) have important functions in shell formation. A novel SMP with a PDZ domain (PDZ-domain-containing-protein-1, PDCP-1) was identified from the shell matrices of Mytilus coruscus. In this study, the gene expression, function, and location of PDCP-1 were analyzed. PDCP-1 was characterized as an ∼70 kDa protein with a PDZ (postsynaptic density/discs large/zonula occludes) domain and a ZM (ZASP-like motif) domain. The PDCP-1 gene has a high expression level and specific location in the foot, mantle and adductor muscle. Recombinantly expressed PDCP-1 (rPDCP-1) altered the morphology of calcite crystals, the polymorph of calcite crystals, binding with both calcite and aragonite crystals, and inhibition of the crystallization rate of calcite crystals. In addition, anti-rPDCP-1 antibody was prepared, and immunohistochemistry and immunofluorescence analyses revealed the specific location of PDCP-1 in the mantle, the adductor muscle, and the aragonite (nacre and myostracum) layer of the shell, suggesting multiple functions of PDCP-1 in biomineralization, muscle-shell attachment, and muscle attraction. Furthermore, pull-down analysis revealed 19 protein partners of PDCP-1 from the shell matrices, which accordingly provided a possible interaction network of PDCP-1 in the shell. These results expand the understanding of the functions of PDZ-domain-containing proteins (PDCPs) in biomineralization and the supramolecular chemistry that contributes to shell formation.

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Microstructure and in-depth proteomic analysis of Perna viridis shell

Cited by 31 publications

References 94 publications

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

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

Molecular characterization of a whirlin-like protein with biomineralization-related functions from the shell of Mytilus coruscus

Molecular Characterization of a Novel Shell Matrix Protein With PDZ Domain From Mytilus coruscus

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