Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell

• Published in: PloS one Vol. 10; no. 7; p. e0133866
• Main Authors: Zhang, Gen, He, Li-Sheng, Wong, Yue-Him, Xu, Ying, Zhang, Yu, Qian, Pei-Yuan
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 29-07-2015; Public Library of Science (PLoS)
• Subjects: Amino Acid Sequence; Amino acids; Animal Shells - anatomy & histology; Animal Shells - chemistry; Animal Shells - metabolism; Animals; Arthropod Proteins - chemistry; Arthropod Proteins - metabolism; Balanus; Balanus amphitrite; Biofouling; Carbonic anhydrase; Carbonic anhydrases; Cellular proteins; Chemical composition; Chorion; Crustaceans; Environmental science; Functional groups; Genetic aspects; Hardness; Histology; Identification and classification; Laboratories; Lectins; Life sciences; Matrix protein; Methods; Molecular Sequence Data; Peroxidase; Proteinase; Proteins; Proteomics; Serine; Sessilia; Shells; Thoracica - anatomy & histology; Thoracica - metabolism
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0133866

As 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.