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Shell matrix protein of estuarine oyster (Crassostrea ariakensis) and Pacific oyster (Crassostrea gigas)

ABSTRACT: Studying the adaptive divergence of shellfish inhabiting different environments is crucial to predict the resilience of marine organisms to rapid climate change. Although the shell serves as the primary physical barrier against environmental change, the evolutionary adaptation of biomineralization in shellfish remains poorly understood. In this study, we using common garden designs to investigate the shell matrix proteome of estuarine (Crassostrea ariakensis) and Pacific (Crassostrea gigas) oysters inhabiting estuarine and open coastal zones, respectively. Shell matrix proteome analyses revealed extensive domain expansion of classical pathway secretomes, which likely contribute to the enhanced biomineralization capacity of estuarine oysters. Furthermore, two-thirds of the 27 C. ariakensis-specific shell matrix-secreted proteins (SMSPs) lacked homology with known proteins in the Swiss-Prot and nr databases, indicating rapid evolution. Our findings suggest that intensified classical pathway secretomes and rapid evolution of species-specific SMSPs are key factors shaping the defense of shells to enhance their adaptive potential to climate change.

INSTRUMENT(S):

ORGANISM(S): Crassostrea Ariakensis Crassostrea Gigas (pacific Oyster) (crassostrea Angulata)

TISSUE(S): Exoskeleton

SUBMITTER: shentong wang

LAB HEAD: shentong wang

PROVIDER: PXD053708 | Pride | 2026-03-29

REPOSITORIES: Pride

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Project description:Background: The shells of various Haliotis species have served as models of invertebrate biomineralization and physical shell properties for more than 20 years. A focus of this research has been the nacreous inner layer of the shell with its conspicuous arrangement of aragonite platelets, resembling in cross-section a brick-and-mortar wall. In comparison, the outer, less stable, calcitic prismatic layer has received much less attention. One of the first molluscan shell proteins to be characterized at the molecular level was Lustrin A, a component of the nacreous organic matrix of Haliotis rufescens. This was soon followed by the C-type lectin perlucin and the growth factor-binding perlustrin, both isolated from H. laevigata nacre, and the crystal growth-modulating AP7 and AP24, isolated from H. rufescens nacre. Mass spectrometry-based proteomics was subsequently applied to to Haliotis biomineralization research with the analysis of the H. asinina shell matrix and yielded 14 different shell-associated proteins. That study was the most comprehensive for a Haliotis species to date. Methods: The shell proteomes of nacre and prismatic layer of the marine gastropod Haliotis laevigata were analyzed combining mass spectrometry-based proteomics and next generation sequencing. Results: We identified 297 proteins from the nacreous shell layer and 350 proteins from the prismatic shell layer from the green lip abalone H. laevigata. Considering the overlap between the two sets we identified a total of 448 proteins. Fifty-one nacre proteins and 43 prismatic layer proteins were defined as major proteins based on their abundance at more than 0.2% of the total. The remaining proteins occurred at low abundance and may not play any significant role in shell fabrication. The overlap of major proteins between the two shell layers was 17, amounting to a total of 77 major proteins. Conclusions: The H. laevigata shell proteome shares moderate sequence similarity at the protein level with other gastropod, bivalve and more distantly related invertebrate biomineralising proteomes. Features conserved in H. laevigata and other molluscan shell proteomes include short repetitive sequences of low complexity predicted to lack intrinsic three-dimensional structure, and domains such as tyrosinase, chitin-binding, and carbonic anhydrase. This catalogue of H. laevigata shell proteins represents the most comprehensive for a haliotid and should support future efforts to elucidate the molecular mechanisms of shell assembly.

			Action	DRS
	22072905_WS_BURONG-AR.raw	Raw
	22072905_WS_BURONG-GI.raw	Raw
	22072905_WS_kerong-AR.raw	Raw
	22072905_WS_kerong-GI.raw	Raw
	ar_proteinGroups.txt	Txt

Dataset Information

Shell matrix protein of estuarine oyster (Crassostrea ariakensis) and Pacific oyster (Crassostrea gigas)

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