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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 the carbonic anhydrase from Amphibalanus amphitrite (I, II and III), Daphnia pulex (EFX81683.1), Danio rerio (NP571185.1) and Hyriopsis cumingii (AHY35316.1).Putative histidine residues that function as zinc ligands are marked with filled circles above the residues. The residues forming the hydrogen-bonded network to zinc-bound solvent molecules are depicted by open circles.
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pone.0133866.g004: Alignment of the carbonic anhydrase from Amphibalanus amphitrite (I, II and III), Daphnia pulex (EFX81683.1), Danio rerio (NP571185.1) and Hyriopsis cumingii (AHY35316.1).Putative histidine residues that function as zinc ligands are marked with filled circles above the residues. The residues forming the hydrogen-bonded network to zinc-bound solvent molecules are depicted by open circles.

Mentions: In the barnacle shell, three homologs of carbonic anhydrase were detected. The first one (coded by CL15286.Contig1_Ba_mix; A. amphitrite I) was detected in all three fractions. Its partial sequence, containing 278 amino acid residues, showed 30% identity with alpha-carbonic anhydrase from Daphnia pulex (EFX81683.1). The second (coded by CL10121.Contig1_Ba_mix; A. amphitrite II) and third (coded by Unigene27659_Ba_mix; A. amphitrite III) proteins both showed 26% and 30% identity with D. pulex alpha-carbonic anhydrase, respectively, and were found in the 1% and 10% SDS fractions. All three putative histidine residues that function as zinc ligands [16] were conserved in carbonic anhydrase II, similarly to the majority of the residues forming the hydrogen-bond network to zinc-bound solvent molecules (Fig 4). However, for carbonic anhydrase I and III, two of the three histidines that function as zinc ligands were mutated (Fig 4).


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 the carbonic anhydrase from Amphibalanus amphitrite (I, II and III), Daphnia pulex (EFX81683.1), Danio rerio (NP571185.1) and Hyriopsis cumingii (AHY35316.1).Putative histidine residues that function as zinc ligands are marked with filled circles above the residues. The residues forming the hydrogen-bonded network to zinc-bound solvent molecules are depicted by open circles.
© Copyright Policy
Related In: Results  -  Collection

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

pone.0133866.g004: Alignment of the carbonic anhydrase from Amphibalanus amphitrite (I, II and III), Daphnia pulex (EFX81683.1), Danio rerio (NP571185.1) and Hyriopsis cumingii (AHY35316.1).Putative histidine residues that function as zinc ligands are marked with filled circles above the residues. The residues forming the hydrogen-bonded network to zinc-bound solvent molecules are depicted by open circles.
Mentions: In the barnacle shell, three homologs of carbonic anhydrase were detected. The first one (coded by CL15286.Contig1_Ba_mix; A. amphitrite I) was detected in all three fractions. Its partial sequence, containing 278 amino acid residues, showed 30% identity with alpha-carbonic anhydrase from Daphnia pulex (EFX81683.1). The second (coded by CL10121.Contig1_Ba_mix; A. amphitrite II) and third (coded by Unigene27659_Ba_mix; A. amphitrite III) proteins both showed 26% and 30% identity with D. pulex alpha-carbonic anhydrase, respectively, and were found in the 1% and 10% SDS fractions. All three putative histidine residues that function as zinc ligands [16] were conserved in carbonic anhydrase II, similarly to the majority of the residues forming the hydrogen-bond network to zinc-bound solvent molecules (Fig 4). However, for carbonic anhydrase I and III, two of the three histidines that function as zinc ligands were mutated (Fig 4).

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.