Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell
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AbstractAs typical biofoulers, barnacles possess hard shells and cause serious biofouling problems. In this study, we analyzed the protein component of the barnacle Amphibalanus (= Balanus) amphitrite shell using gel-based proteomics. The results revealed 52 proteins in the A. Amphitrite shell. Among them, 40 proteins were categorized into 11 functional groups based on KOG database, and the remaining 12 proteins were unknown. Besides the known proteins in barnacle shell (SIPC, carbonic anhydrase and acidic acid matrix protein), we also identified chorion peroxidase, C-type lectin-like domains, serine proteases and proteinase inhibitor proteins in the A. Amphitrite shell. The sequences of these proteins were characterized and their potential functions were discussed. Histology and DAPI staining revealed living cells in the shell, which might secrete the shell proteins identified in this study.
CitationZhang, G., He, L., Wong, Y.-H., Xu, Y., Zhang, Y., & Qian, P. (2015). Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell. PLOS ONE, 10(7), e0133866. doi:10.1371/journal.pone.0133866
SponsorsThis work was supported by a grant (DY125-15-T-02) from the China Ocean Mineral Resources Research and Development Association, an award from the King Abdullah University of Science and Technology (SA-C0040/UK-C0016) and grants (GRF661611, GRF662413) from the Research Grants Council of the Hong Kong Special Administrative Region to PYQ as well as a grant from the National Natural Science Foundation of China (31460092) to LSH. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
PublisherPUBLIC LIBRARY SCIENCE
PubMed Central IDPMC4519255
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