Review: Post-translational modifications of marine shell matrix proteins

Rivera-Pérez, Crisalejandra; Hernández-Saavedra, Norma Y.

doi:10.1016/j.cbpb.2021.110641

Cited by 7 publications

(6 citation statements)

References 103 publications

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“…Shell matrix proteins, components of this organic matrix, control the necessary biomineralisation process [ 10 ]. Posttranslational modifications of these proteins, including glycosylation, often contribute to this process by modulating the protein activity [ 11 ]. The significance of glycoproteins in the biomineralisation process could be confirmed clearly by deglycosylation experiments or the comparison of glycosylated with recombinant non-glycosylated versions [ 12 , 13 , 14 ].…”

Section: Shell Matrix Protein Glycosylationmentioning

confidence: 99%

Mollusc N-glycosylation: Structures, Functions and Perspectives

Staudacher

2021

Biomolecules

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Molluscs display a sophisticated N-glycan pattern on their proteins, which is, in terms of involved structural features, even more diverse than that of vertebrates. This review summarises the current knowledge of mollusc N-glycan structures, with a focus on the functional aspects of the corresponding glycoproteins. Furthermore, the potential of mollusc-derived biomolecules for medical applications is addressed, emphasising the importance of mollusc research.

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Section: Shell Matrix Protein Glycosylationmentioning

confidence: 99%

Mollusc N-glycosylation: Structures, Functions and Perspectives

Staudacher

2021

Biomolecules

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“…Availability of the gene sequences was evaluated with C. gigas CDS and NCBInr databases. The disparity of the molecular masses between the observed and theoretical mass may be due to the additional presence of post-translational modifications [ 44 ].…”

Section: Resultsmentioning

confidence: 99%

“…Those that could not bind to the lectin might have flowed through together with other protein components in the unbound fraction. On the other hand, the 43 and 48 kDa bands which could only be visualized with Stains-all staining were not successfully identified due to a lack of tryptic cleavage sites and also due to stain interference [ 44 ].…”

Section: Resultsmentioning

confidence: 99%

“…Conversely, under non-reducing conditions, significant settlement-inducing activities were observed at the 35, 38, and 48 kDa polypeptide bands ( Supplementary text A.3, Figure S4 ). This suggests that disulfide bonds might be necessary for the folding and stabilization of the settlement-inducing factors in this cue [ 44 ].…”

Section: Resultsmentioning

confidence: 99%

“…Several molluscan shell matrix proteins (SMPs) have been recently identified in shells, including that of C. gigas , but much of the focus has been on their biomineralization roles [ 41 , 42 ]. One of the main challenges to studying SMPs is their inherent difficulty to isolate, characterize and obtain enough of an amount for functional analyses due to their close association with the mineral phase, highly charged nature, and presence of post-translational modifications (PTMs) [ 43 , 44 ]. To overcome this, a larval settlement-guided approach was developed to locate the signal molecule from C. gigas conspecific shells, aided by various biochemical analyses using different gel staining methods and enzyme treatments, mass spectrometry analyses, bioinformatics analyses of protein sequences, and gene expression analysis of a selected gene between the C. gigas pediveliger and postlarvae.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Characterization of the Larval Settlement Pheromone Protein Components in Adult Shells of Crassostrea gigas: A Novel Function of Shell Matrix Proteins

Sedanza

Yoshida

Kim

et al. 2022

IJMS

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The global decline of natural oyster populations emphasizes the need to improve our understanding of their biology. Understanding the role of chemical cues from conspecifics on how oysters occupy appropriate substrata is crucial to learning about their evolution, population dynamics, and chemical communication. Here, a novel role of a macromolecular assembly of shell matrix proteins which act as Crassostrea gigas Settlement Pheromone Protein Components in adult shells is demonstrated as the biological cue responsible for gregarious settlement on conspecifics. A bioassay-guided fractionation approach aided by biochemical and molecular analyses reveals that Gigasin-6 isoform X1 and/or X2 isolated from adult shells is the major inducing cue for larval settlement and may also play a role in postlarva–larva settlement interactions. Other isolated Stains-all-stainable acidic proteins may function as a co-factor and a scaffold/structural framework for other matrix proteins to anchor within this assembly and provide protection. Notably, conspecific cue-mediated larval settlement induction in C. gigas presents a complex system that requires an interplay of different glycans, disulfide bonds, amino acid groups, and phosphorylation crosstalk for recognition. These results may find application in the development of oyster aquacultures which could help recover declining marine species and as targets of anti-fouling agents.

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