scholarly journals The ‘Shellome’ of the Crocus Clam Tridacna crocea Emphasizes Essential Components of Mollusk Shell Biomineralization

2021 ◽  
Vol 12 ◽  
Author(s):  
Takeshi Takeuchi ◽  
Manabu Fujie ◽  
Ryo Koyanagi ◽  
Laurent Plasseraud ◽  
Isabelle Ziegler-Devin ◽  
...  

Molluscan shells are among the most fascinating research objects because of their diverse morphologies and textures. The formation of these delicate biomineralized structures is a matrix-mediated process. A question that arises is what are the essential components required to build these exoskeletons. In order to understand the molecular mechanisms of molluscan shell formation, it is crucial to identify organic macromolecules in different shells from diverse taxa. In the case of bivalves, however, taxon sampling in previous shell proteomics studies are focused predominantly on representatives of the class Pteriomorphia such as pearl oysters, edible oysters and mussels. In this study, we have characterized the shell organic matrix from the crocus clam, Tridacna crocea, (Heterodonta) using various biochemical techniques, including SDS-PAGE, FT-IR, monosaccharide analysis, and enzyme-linked lectin assay (ELLA). Furthermore, we have identified a number of shell matrix proteins (SMPs) using a comprehensive proteomics approach combined to RNA-seq. The biochemical studies confirmed the presence of proteins, polysaccharides, and sulfates in the T. crocea shell organic matrix. Proteomics analysis revealed that the majority of the T. crocea SMPs are novel and dissimilar to known SMPs identified from the other bivalve species. Meanwhile, the SMP repertoire of the crocus clam also includes proteins with conserved functional domains such as chitin-binding domain, VWA domain, and protease inhibitor domain. We also identified BMSP (Blue Mussel Shell Protein, originally reported from Mytilus), which is widely distributed among molluscan shell matrix proteins. Tridacna SMPs also include low-complexity regions (LCRs) that are absent in the other molluscan genomes, indicating that these genes may have evolved in specific lineage. These results highlight the diversity of the organic molecules – in particular proteins – that are essential for molluscan shell formation.




2016 ◽  
Vol 27 ◽  
pp. 69-74 ◽  
Author(s):  
Jaison Arivalagan ◽  
Benjamin Marie ◽  
Victoria A. Sleight ◽  
Melody S. Clark ◽  
Sophie Berland ◽  
...  


CrystEngComm ◽  
2018 ◽  
Vol 20 (27) ◽  
pp. 3905-3916 ◽  
Author(s):  
Jinzhe Du ◽  
Guangrui Xu ◽  
Chuang Liu ◽  
Rongqing Zhang

Phosphorylation of shell matrix proteins is critical for shell formation in vivo and can modulate calcium carbonate formation in vitro.



2006 ◽  
Vol 62 (3) ◽  
pp. 307-318 ◽  
Author(s):  
Isao Sarashina ◽  
Haruyo Yamaguchi ◽  
Takuma Haga ◽  
Minoru Iijima ◽  
Satoshi Chiba ◽  
...  


Author(s):  
Yinghui Ji ◽  
Xue Yang ◽  
Dong Yang ◽  
Rongqing Zhang

AbstractBiomineralization is a widespread biological process, involved in the formation of shells, teeth, and bones. Shell matrix proteins have been widely studied for their importance during shell formation. In 2015, our group identified 72 unique shell matrix proteins in Pinctada fucata, among which PU14 is a matrix protein detected in the soluble fraction that solely exists in the prismatic layer. However, the function of PU14 is still unclear. In this study, the full-length cDNA sequence of PU14 was obtained and functional analyses of PU14 protein during shell formation were performed. The deduced protein has a molecular mass of 77.8 kDa and an isoelectric point of 11.34. The primary protein structure contains Gln-rich and random repeat units, which are typical characteristics of matrix protein and indicate its potential function during shell formation. In vivo and in vitro experiments indicated PU14 has prismatic layer functions during shell formation. The tissue expression patterns showed that PU14 was mainly expressed in the mantle tissue, which is consistent with prismatic layer formation. Notching experiments suggested that PU14 responded to repair and regenerate the injured shell. After inhibiting gene expression by injecting PU14-specific double-stranded RNA, the inner surface of the prismatic layer changed significantly and became rougher. Further, in vitro experiments showed that recombinant protein rPU14 impacted calcite crystal morphology. Taken together, characterization and functional analyses of a novel matrix protein, PU14, provide new insights about basic matrix proteins and their functions during shell formation.



2016 ◽  
Vol 12 (05) ◽  
pp. 266-278 ◽  
Author(s):  
Abhishek Upadhyay ◽  
◽  
Vengatesen Thiyagarajan ◽  
◽  
◽  
...  


2019 ◽  
Vol 286 (1916) ◽  
pp. 20192043 ◽  
Author(s):  
A. Miglioli ◽  
R. Dumollard ◽  
T. Balbi ◽  
L. Besnardeau ◽  
L. Canesi

Bivalve biomineralization is a highly complex and organized process, involving several molecular components identified in adults and larval stages. However, information is still scarce on the ontogeny of the organic matrix before calcification occurs. In this work, first shell formation was investigated in the mussel Mytilus galloprovincialis . The time course of organic matrix and CaCO 3 deposition were followed at close times post fertilization (24, 26, 29, 32, 48 h) by calcofluor and calcein staining, respectively. Both components showed an exponential trend in growth, with a delay between organic matrix and CaCO 3 deposition. mRNA levels of genes involved in matrix deposition (chitin synthase; tyrosinase- TYR) and calcification (carbonic anhydrase; extrapallial protein) were quantified by qPCR at 24 and 48 hours post fertilization (hpf) with respect to eggs. All transcripts were upregulated across early development, with TYR showing highest mRNA levels from 24 hpf. TYR transcripts were closely associated with matrix deposition as shown by in situ hybridization. The involvement of tyrosinase activity was supported by data obtained with the enzyme inhibitor N-phenylthiourea. Our results underline the pivotal role of shell matrix in driving first CaCO 3 deposition and the importance of tyrosinase in the formation of the first shell in M. galloprovincialis .







2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Chuang Liu ◽  
Shiguo Li ◽  
Jingjing Kong ◽  
Yangjia Liu ◽  
Tianpeng Wang ◽  
...  


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