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

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,...

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Bibliographic Details
Published in:PloS one 2015-07, Vol.10 (7), p.e0133866-e0133866
Main Authors: Zhang, Gen, He, Li-Sheng, Wong, Yue-Him, Xu, Ying, Zhang, Yu, Qian, Pei-Yuan
Format: Article
Language:English
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
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0133866