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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.


Comparison of an Asp-rich shell matrix protein from Amphibalanus amphitrite with Asprich (Atrina rigida; AAU04808.1) and Aspein (Pinctada fucata; AB094512).The Asp-rich shell matrix protein from A. amphitrite mainly contained Asp punctuated with Glu or Gly, which are labeled in bold with a single underline. Asprich includes three poly(Asp) motifs (presented in block with a single underline) and two DEAD motifs (presented in bold with a double underline). Aspein consists of mostly poly(Asp) blocks punctuated with Ser-Gly dipeptides (presented in bold with a single underline).
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pone.0133866.g002: Comparison of an Asp-rich shell matrix protein from Amphibalanus amphitrite with Asprich (Atrina rigida; AAU04808.1) and Aspein (Pinctada fucata; AB094512).The Asp-rich shell matrix protein from A. amphitrite mainly contained Asp punctuated with Glu or Gly, which are labeled in bold with a single underline. Asprich includes three poly(Asp) motifs (presented in block with a single underline) and two DEAD motifs (presented in bold with a double underline). Aspein consists of mostly poly(Asp) blocks punctuated with Ser-Gly dipeptides (presented in bold with a single underline).

Mentions: An acidic shell matrix protein (coded by CL6615.Contig1_Ba_mix) was identified in the acetic acid fraction (Fig 2). This protein did not retrieve any known proteins using Blastp or tBlastn in NCBI. The partial sequence (381 amino acids) was used to calculate the most dominant amino acids, where were Asp (41.2%), Glu (21.8%) and Gly (14.2%) (S2 Table). The pI was estimated at 2.68. Compared with Asprich from A. rigida, this protein displayed an identity of 38.6% and a similarity of 49.0%; a slightly lower similarity (31.8%) and identity (43.7%) were obtained for this protein compared to Aspein from P. fucata.


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)

Comparison of an Asp-rich shell matrix protein from Amphibalanus amphitrite with Asprich (Atrina rigida; AAU04808.1) and Aspein (Pinctada fucata; AB094512).The Asp-rich shell matrix protein from A. amphitrite mainly contained Asp punctuated with Glu or Gly, which are labeled in bold with a single underline. Asprich includes three poly(Asp) motifs (presented in block with a single underline) and two DEAD motifs (presented in bold with a double underline). Aspein consists of mostly poly(Asp) blocks punctuated with Ser-Gly dipeptides (presented in bold with a single underline).
© Copyright Policy
Related In: Results  -  Collection

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

pone.0133866.g002: Comparison of an Asp-rich shell matrix protein from Amphibalanus amphitrite with Asprich (Atrina rigida; AAU04808.1) and Aspein (Pinctada fucata; AB094512).The Asp-rich shell matrix protein from A. amphitrite mainly contained Asp punctuated with Glu or Gly, which are labeled in bold with a single underline. Asprich includes three poly(Asp) motifs (presented in block with a single underline) and two DEAD motifs (presented in bold with a double underline). Aspein consists of mostly poly(Asp) blocks punctuated with Ser-Gly dipeptides (presented in bold with a single underline).
Mentions: An acidic shell matrix protein (coded by CL6615.Contig1_Ba_mix) was identified in the acetic acid fraction (Fig 2). This protein did not retrieve any known proteins using Blastp or tBlastn in NCBI. The partial sequence (381 amino acids) was used to calculate the most dominant amino acids, where were Asp (41.2%), Glu (21.8%) and Gly (14.2%) (S2 Table). The pI was estimated at 2.68. Compared with Asprich from A. rigida, this protein displayed an identity of 38.6% and a similarity of 49.0%; a slightly lower similarity (31.8%) and identity (43.7%) were obtained for this protein compared to Aspein from P. fucata.

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.