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

Zhang G, He LS, Wong YH, Xu Y, Zhang Y, Qian PY - PLoS ONE (2015)

Bottom Line: The results revealed 52 proteins in the A.Amphitrite shell.

View Article: PubMed Central - PubMed

Affiliation: Environmental Science Programs and Division of Life Science, School of Science, The Hong Kong University of Science and Technology, Clearwater Bay, Kowloon, Hong Kong SAR, R. P. China.

ABSTRACT
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.

No MeSH data available.


Alignment of C-type lectin-like domains from Amphibalanus amphitrite (I and II), Scylla paramamosain (ADF27340.1), Fenneropenaeus indicus (ADV17348.1), Litopenaeus vannamei (AGV68681.1), and Danio rerio (XP005172687.1).Similarly to S. paramamosain and F. indicus, the typical "EPD" or "EPN" motif in both C-type lectin-like domains (I and II) was mutated into "QPD" in A. amphitrite (boxed in red). At least two and four cysteines were conserved in the C-type lectin-like domains I and II, respectively. These conserved cysteines are indicated by arrows.
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pone.0133866.g006: Alignment of C-type lectin-like domains from Amphibalanus amphitrite (I and II), Scylla paramamosain (ADF27340.1), Fenneropenaeus indicus (ADV17348.1), Litopenaeus vannamei (AGV68681.1), and Danio rerio (XP005172687.1).Similarly to S. paramamosain and F. indicus, the typical "EPD" or "EPN" motif in both C-type lectin-like domains (I and II) was mutated into "QPD" in A. amphitrite (boxed in red). At least two and four cysteines were conserved in the C-type lectin-like domains I and II, respectively. These conserved cysteines are indicated by arrows.

Mentions: Two proteins containing a C-type lectin-like domain were detected in the shell of A. amphitrite. Among them, the protein coded by CL14971.Contig1_Ba_mix was present in all three fractions, while the protein coded by Unigene5283_Ba_mix was detected in the 1% SDS fraction. After searching NCBI, both proteins were found to be the most similar to the mannose-binding protein from the mud crab Scylla paramamosain, with a similarity of 22.5% and 18.8%, respectively. Alignment with the C-type lectin-like domains from other animals revealed that both C-type lectin-like domains found in this study included a "QPD" motif in the Ca2+-binding site and 2 or 4 conserved cysteine residues (Fig 6).


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

Zhang G, He LS, Wong YH, Xu Y, Zhang Y, Qian PY - PLoS ONE (2015)

Alignment of C-type lectin-like domains from Amphibalanus amphitrite (I and II), Scylla paramamosain (ADF27340.1), Fenneropenaeus indicus (ADV17348.1), Litopenaeus vannamei (AGV68681.1), and Danio rerio (XP005172687.1).Similarly to S. paramamosain and F. indicus, the typical "EPD" or "EPN" motif in both C-type lectin-like domains (I and II) was mutated into "QPD" in A. amphitrite (boxed in red). At least two and four cysteines were conserved in the C-type lectin-like domains I and II, respectively. These conserved cysteines are indicated by arrows.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4519255&req=5

pone.0133866.g006: Alignment of C-type lectin-like domains from Amphibalanus amphitrite (I and II), Scylla paramamosain (ADF27340.1), Fenneropenaeus indicus (ADV17348.1), Litopenaeus vannamei (AGV68681.1), and Danio rerio (XP005172687.1).Similarly to S. paramamosain and F. indicus, the typical "EPD" or "EPN" motif in both C-type lectin-like domains (I and II) was mutated into "QPD" in A. amphitrite (boxed in red). At least two and four cysteines were conserved in the C-type lectin-like domains I and II, respectively. These conserved cysteines are indicated by arrows.
Mentions: Two proteins containing a C-type lectin-like domain were detected in the shell of A. amphitrite. Among them, the protein coded by CL14971.Contig1_Ba_mix was present in all three fractions, while the protein coded by Unigene5283_Ba_mix was detected in the 1% SDS fraction. After searching NCBI, both proteins were found to be the most similar to the mannose-binding protein from the mud crab Scylla paramamosain, with a similarity of 22.5% and 18.8%, respectively. Alignment with the C-type lectin-like domains from other animals revealed that both C-type lectin-like domains found in this study included a "QPD" motif in the Ca2+-binding site and 2 or 4 conserved cysteine residues (Fig 6).

Bottom Line: The results revealed 52 proteins in the A.Amphitrite shell.

View Article: PubMed Central - PubMed

Affiliation: Environmental Science Programs and Division of Life Science, School of Science, The Hong Kong University of Science and Technology, Clearwater Bay, Kowloon, Hong Kong SAR, R. P. China.

ABSTRACT
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.

No MeSH data available.