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Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
The barnacle, Amphibalanus amphitrite, is a common marine fouling organism. Understanding the mechanism of barnacle adhesion will be helpful in resolving the fouling problem. Barnacle cement is thought to play a key role in barnacle attachment. Although several adult barnacle cement proteins have be...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3661472/ https://www.ncbi.nlm.nih.gov/pubmed/23717550 http://dx.doi.org/10.1371/journal.pone.0064130 |
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author | He, Li-Sheng Zhang, Gen Qian, Pei-Yuan |
author_facet | He, Li-Sheng Zhang, Gen Qian, Pei-Yuan |
author_sort | He, Li-Sheng |
collection | PubMed |
description | The barnacle, Amphibalanus amphitrite, is a common marine fouling organism. Understanding the mechanism of barnacle adhesion will be helpful in resolving the fouling problem. Barnacle cement is thought to play a key role in barnacle attachment. Although several adult barnacle cement proteins have been identified in Megabalanus rosa, little is known about their function in barnacle settlement. In this study, two homologous 20k-cement proteins (cp20k) in Amphibalanus amphitrite, named Bamcp20k-1 and Bamcp20k-2, were characterized. The two homologues share primary sequence structure with proteins from other species including Megabalanus rosa and Fistulobalanus albicostatus. The conserved structure included repeated Cys domains and abundant charged amino acids, such as histidine. In this study we demonstrated that Bamcp20k-1 localized at the α secretory cells in the cyprid cement gland, while Bamcp20k-2 localized to the β secretory cells. The differential localizations suggest differential regulation for secretion from the secretory cells. Both Bamcp20k-1 and Bamcp20k-2 from cyprids dissolved in PBS. However, adult Bamcp20k-2, which was dominant in the basal shell of adult barnacles, was largely insoluble in PBS. Solubility increased in the presence of the reducing reagent Dithiothreitol (DTT), suggesting that the formation of disulfide bonds plays a role in Bamcp20k-2 function. In comparison, Bamcp20k-1, which was enriched in soft tissue, could not be easily detected in the shell and base by Western blot and easily dissolved in PBS. These differential solubilities and localizations indicate that Bamcp20k-1 and Bamcp20k-2 have distinct functions in barnacle cementing. |
format | Online Article Text |
id | pubmed-3661472 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-36614722013-05-28 Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite He, Li-Sheng Zhang, Gen Qian, Pei-Yuan PLoS One Research Article The barnacle, Amphibalanus amphitrite, is a common marine fouling organism. Understanding the mechanism of barnacle adhesion will be helpful in resolving the fouling problem. Barnacle cement is thought to play a key role in barnacle attachment. Although several adult barnacle cement proteins have been identified in Megabalanus rosa, little is known about their function in barnacle settlement. In this study, two homologous 20k-cement proteins (cp20k) in Amphibalanus amphitrite, named Bamcp20k-1 and Bamcp20k-2, were characterized. The two homologues share primary sequence structure with proteins from other species including Megabalanus rosa and Fistulobalanus albicostatus. The conserved structure included repeated Cys domains and abundant charged amino acids, such as histidine. In this study we demonstrated that Bamcp20k-1 localized at the α secretory cells in the cyprid cement gland, while Bamcp20k-2 localized to the β secretory cells. The differential localizations suggest differential regulation for secretion from the secretory cells. Both Bamcp20k-1 and Bamcp20k-2 from cyprids dissolved in PBS. However, adult Bamcp20k-2, which was dominant in the basal shell of adult barnacles, was largely insoluble in PBS. Solubility increased in the presence of the reducing reagent Dithiothreitol (DTT), suggesting that the formation of disulfide bonds plays a role in Bamcp20k-2 function. In comparison, Bamcp20k-1, which was enriched in soft tissue, could not be easily detected in the shell and base by Western blot and easily dissolved in PBS. These differential solubilities and localizations indicate that Bamcp20k-1 and Bamcp20k-2 have distinct functions in barnacle cementing. Public Library of Science 2013-05-22 /pmc/articles/PMC3661472/ /pubmed/23717550 http://dx.doi.org/10.1371/journal.pone.0064130 Text en © 2013 He et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article He, Li-Sheng Zhang, Gen Qian, Pei-Yuan Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite |
title | Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
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title_full | Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
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title_fullStr | Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
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title_full_unstemmed | Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
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title_short | Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
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title_sort | characterization of two 20kda-cement protein (cp20k) homologues in amphibalanus amphitrite |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3661472/ https://www.ncbi.nlm.nih.gov/pubmed/23717550 http://dx.doi.org/10.1371/journal.pone.0064130 |
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