In-depth proteomic analysis of nacre, prism, and myostracum of Mytilus shell

Liao, Zhi; Bao, Lin-fei; Fan, Meihua; Gao, Peng; Wang, Xinxing; Qin, Chuanli; Li, Xiaomin

doi:10.1016/j.jprot.2015.03.027

Cited by 94 publications

(124 citation statements)

References 57 publications

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“…We noticed that all conceptually translated EST sequences that match the MS/MS peptides present a signal peptide, when the sequence exhibits a complete N-terminus, suggesting that these proteins are all secreted by the mantle epithelia through a classical cellular secretion pathway. This list of nacre proteins is among the largest nacre SMP sets described so far, and is comparable to the published SMP set from Pinctada and Mytilus models, which have 35 and 42 proteins, respectively [16][17][18]. While the present results confirm the presence of previously described protein domains, such as Pif, CA, Kunitz-like, WAP, M-rich, Q-rich, A-rich or chitinbinding domains [21,23,24], in a unionoid shell nacre matrix, they also contribute to consistently extend the list of proteins associated with the nacre microstructure.…”

Section: Protein Composition Of Unionoid Nacre Matricessupporting

confidence: 62%

“…Since the initial description of the primary structure of a mollusc shell protein in 1996 [15], numerous nacre-associated proteins have been described so far, mainly from three principal models: the pearl oyster [2,16] and the edible mussel for bivalves [17,18], and the abalone for gastropods [19]. Comparison of their respective nacre biomineralization toolkits from the pearl mussel Pinctada maxima and the abalone Haliotis asinina underlined unexpectedly very few sequence similarities, suggesting either that the bivalves and gastropods independently acquired the capacity to synthesize nacre or that these proteins present a rapid evolution rate, especially in abalone, leading to functional conservation of the respective nacre shell matrix protein sets with only limited primary structure similarities [20].…”

Section: Nacre Proteinsmentioning

confidence: 99%

“…p and m exponents indicate that the protein was also detected in the prismatic shell layer of either Pinctada spp. or Mytilus spp., respectively [2,15,17,18]. (Online version in colour.)…”

Section: Inherited Set Of Nacre and Shell Matrix Proteins In Bivalvesmentioning

confidence: 99%

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Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa

Marie

Arivalagan

Matheron

et al. 2017

J. R. Soc. Interface.

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The formation of the molluscan shell nacre is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell-forming tissue, the mantle. This so-called ‘calcifying matrix’ is a complex mixture of proteins, glycoproteins and polysaccharides that is assembled and occluded within the mineral phase during the calcification process. Better molecular-level characterization of the substances that regulate nacre formation is still required. Notable advances in expressed tag sequencing of freshwater mussels, such as Elliptio complanata and Villosa lienosa , provide a pre-requisite to further characterize bivalve nacre proteins by a proteomic approach. In this study, we have identified a total of 48 different proteins from the insoluble matrices of the nacre, 31 of which are common to both E. complanata and V. lienosa . A few of these proteins, such as PIF, MSI60, CA, shematrin-like, Kunitz-like, LamG, chitin-binding-containing proteins, together with A-, D-, G-, M- and Q-rich proteins, appear to be analogues, if not true homologues, of proteins previously described from the pearl oyster or the edible mussel nacre matrices, thus forming a remarkable list of deeply conserved nacre proteins. This work constitutes a comprehensive nacre proteomic study of non-pteriomorphid bivalves that has enabled us to describe the molecular basis of a deeply conserved biomineralization toolkit among nacreous shell-bearing bivalves, with regard to proteins associated with other shell microstructures, with those of other mollusc classes (gastropods, cephalopods) and, finally, with other lophotrochozoans (brachiopods).

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Section: Protein Composition Of Unionoid Nacre Matricessupporting

confidence: 62%

Section: Nacre Proteinsmentioning

confidence: 99%

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Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa

Marie

Arivalagan

Matheron

et al. 2017

J. R. Soc. Interface.

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“…It can deduced from the results in Table 1 that a shell matrix protein reported for M. coruscus 23 known as protease inhibitor‐like protein‐B1 – henceforth referred to as PILP‐B1 (accession version AKS48146.1; Uniprot identifier A0A0K0YAZ2 (A0A0K0YAZ2_MYTCO) – is the top scored candidate detected in the FPLC‐processed samples. Moreover, there is almost complete agreement between the two software engines and this PILP‐B1 protein was also identified in samples obtained by IC.…”

Section: Resultsmentioning

confidence: 99%

“…The existence of protease inhibitor‐like proteins within the shell organic matrix is not new in mollusk 23, 53, 54, including serpin‐like proteins 23, 55. Proteinase inhibitors were found to be highly specific and abundant in shells in Crassostrea gigas 55.…”

Section: Discussionmentioning

confidence: 99%

MSP22.8 is a protease inhibitor‐like protein involved in shell mineralization in the edible mussel Mytilus galloprovincialis

Calvo-Iglesias

Pérez-Estévez²,

González-Fernández

2017

FEBS Open Bio

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The mussel shell protein 22.8 (MSP22.8) is recognized by a monoclonal antibody (M22.8) directed against larvae of the mussel Mytilus galloprovincialis. After being secreted by cells of the mantle‐edge epithelium into the extrapallial (EP) space (the gap between the mantle and the shell), the protein is detected in the extrapallial fluid (EPF) and EP hemocytes and finally becomes part of the shell matrix framework in adult specimens of M. galloprovincialis. In the work described here, we show how MSP22.8 is detected in EPF samples from different species of mussels (M. galloprovincialis, Mytilus edulis, and Xenostrobus securis), and also as a shell matrix protein in M. galloprovincialis, Mytilus chilensis, and Perna canaliculus. A multistep purification strategy was employed to isolate the protein from the EPF, which was then analyzed by mass spectrometry in order to identify it. The results indicate that MSP22.8 is a serpin‐like protein that has great similarity with the protease inhibitor‐like protein‐B1, reported previously for Mytilus coruscus. We suggest that MSP22.8 is part of a system offering protection from proteolysis during biomineralization and is also part of the innate immune system in mussels.

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Recombinant transgelin‐like protein 1 fromMytilusshell induces formation of CaCO₃polymorphic crystalsin vitro

et al. 2020

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Transgelin‐like protein 1 (TLP‐1) was identified from the shell of Mytilus coruscus as a novel 19 kDa shell matrix protein with a calponin homology domain. Localization of TLP‐1 in biomineralization‐related tissues was determined. The effects of recombinant TLP‐1 on calcium carbonate crystallization were studied to determine its possible function in shell mineralization.

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In-depth proteomic analysis of nacre, prism, and myostracum of Mytilus shell

Cited by 94 publications

References 57 publications

Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa

Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa

MSP22.8 is a protease inhibitor‐like protein involved in shell mineralization in the edible mussel Mytilus galloprovincialis

Recombinant transgelin‐like protein 1 fromMytilusshell induces formation of CaCO₃polymorphic crystalsin vitro

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In-depth proteomic analysis of nacre, prism, and myostracum of Mytilus shell

Cited by 94 publications

References 57 publications

Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa

Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa

MSP22.8 is a protease inhibitor‐like protein involved in shell mineralization in the edible mussel Mytilus galloprovincialis

Recombinant transgelin‐like protein 1 fromMytilusshell induces formation of CaCO3polymorphic crystalsin vitro

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Recombinant transgelin‐like protein 1 fromMytilusshell induces formation of CaCO₃polymorphic crystalsin vitro