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Proteomic investigation of the blue mussel larval shell organic matrix

Artikel i vetenskaplig tidskrift
Författare A. Carini
T. Koudelka
A. Tholey
E. Appel
S. N. Gorb
F. Melzner
Kirti Ramesh
Publicerad i Journal of Structural Biology
Volym 208
Nummer/häfte 3
Sidor 11
ISSN 1047-8477
Publiceringsår 2019
Publicerad vid Sven Lovén centrum för marina vetenskaper
Sidor 11
Språk en
Länkar dx.doi.org/10.1016/j.jsb.2019.09.00...
Ämnesord Biomineralization, Mussel larvae, Organic matrix, Shell matrix protein, calcium-carbonate, biomineralization processes, protein, calcification, nacre, evolution, aragonite, prism, Biochemistry & Molecular Biology, Biophysics, Cell Biology
Ämneskategorier Biokemi och molekylärbiologi

Sammanfattning

Shell matrix proteins (SMPs) are occluded within molluscan shells and are fundamental to the biological control over mineralization. While many studies have been performed on adult SMPs, those of larval stages remain largely undescribed. Therefore, this study aimed to characterize the larval shell proteome of the blue mussel for the first time and to compare it to adult mussel shell proteomes. Following development of a method for cleaning larval shells of tissue contaminants, 49 SMPs were identified using shotgun proteomics. Twenty-one proteins were independently identified in all samples indicating that they form a subset of the core larval shell proteome. These included: the blue mussel shell protein, a peroxidase domain-containing sequence, a laminin G domain-containing sequence, a ZIP domain-containing sequence and a ferric-chelate reductase 1-like sequence. Additional SMP domains identified were: fibronectin type III, BPTI/Kunitz, chitin-binding type 3, thyroglobulin and EF-hand. While key predictable molluscan shell matrix functions are identified, 67% of sequences remain unknown or uncharacterized, indicating that this shell proteome is unique to mussel larvae. Specifically, comparison with adult mytilids reveals that nine domains are exclusive to the larval shell proteome and only four domains are conserved among species and developmental stages. Thus, strong species-specific and ontogenetic variation exists in shell proteome composition.

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