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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.


Related in: MedlinePlus

Alignment of the deduced chorion peroxidase/peroxinectin from Amphibalanus amphitrite, Acyrthosiphon pisum (XP001946672.2), Eriocheir sinensis (ADF87945.1), Macrophthalmus japonicas (AID47197.1), and Penaeus monodon (AAL05973.1).The putative integrin-binding motif is indicated by a red box, and in A. amphitrite, this motif was mutated to YGD (Tyr-Gly-Asp) rather than the canonical sequence RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp).
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pone.0133866.g005: Alignment of the deduced chorion peroxidase/peroxinectin from Amphibalanus amphitrite, Acyrthosiphon pisum (XP001946672.2), Eriocheir sinensis (ADF87945.1), Macrophthalmus japonicas (AID47197.1), and Penaeus monodon (AAL05973.1).The putative integrin-binding motif is indicated by a red box, and in A. amphitrite, this motif was mutated to YGD (Tyr-Gly-Asp) rather than the canonical sequence RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp).

Mentions: A protein (coded by CL8390.Contig1_Ba_mix) identified in all three extractions showed 34% identity to the chorion peroxidase from the pea aphid Acyrthosiphon pisum (XP001946672.2) and 40% identity to that from the Chinese mitten crab Eriocheir sinensis (also named as peroxinectin; ADF87945.1). One putative integrin-binding motif was located at the C terminus of this protein, and this motif was mutated to YGD (Tyr-Gly-Asp) rather than the canonical sequence RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp) (Fig 5).


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 deduced chorion peroxidase/peroxinectin from Amphibalanus amphitrite, Acyrthosiphon pisum (XP001946672.2), Eriocheir sinensis (ADF87945.1), Macrophthalmus japonicas (AID47197.1), and Penaeus monodon (AAL05973.1).The putative integrin-binding motif is indicated by a red box, and in A. amphitrite, this motif was mutated to YGD (Tyr-Gly-Asp) rather than the canonical sequence RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp).
© Copyright Policy
Related In: Results  -  Collection

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

pone.0133866.g005: Alignment of the deduced chorion peroxidase/peroxinectin from Amphibalanus amphitrite, Acyrthosiphon pisum (XP001946672.2), Eriocheir sinensis (ADF87945.1), Macrophthalmus japonicas (AID47197.1), and Penaeus monodon (AAL05973.1).The putative integrin-binding motif is indicated by a red box, and in A. amphitrite, this motif was mutated to YGD (Tyr-Gly-Asp) rather than the canonical sequence RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp).
Mentions: A protein (coded by CL8390.Contig1_Ba_mix) identified in all three extractions showed 34% identity to the chorion peroxidase from the pea aphid Acyrthosiphon pisum (XP001946672.2) and 40% identity to that from the Chinese mitten crab Eriocheir sinensis (also named as peroxinectin; ADF87945.1). One putative integrin-binding motif was located at the C terminus of this protein, and this motif was mutated to YGD (Tyr-Gly-Asp) rather than the canonical sequence RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp) (Fig 5).

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.


Related in: MedlinePlus