Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite

Handle URI:
http://hdl.handle.net/10754/334590
Title:
Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
Authors:
He, Li-Sheng; Zhang, Gen; Qian, Pei-Yuan
Abstract:
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. © 2013 He et al.
Citation:
He L-S, Zhang G, Qian P-Y (2013) Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite. PLoS ONE 8: e64130. doi:10.1371/journal.pone.0064130.
Publisher:
Public Library of Science
Journal:
PLoS ONE
KAUST Grant Number:
SA-C0040; UK-C0016
Issue Date:
22-May-2013
DOI:
10.1371/journal.pone.0064130
PubMed ID:
23717550
PubMed Central ID:
PMC3661472
Type:
Article
ISSN:
1932-6203
Sponsors:
The authors’ research grant from China Ocean Mineral Resources Research and Development Association (DY125-15-T-02), and King Abdullah University of Science and Technology (SA-C0040/UK-C0016) to P.Y. Qian. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Appears in Collections:
Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorHe, Li-Shengen
dc.contributor.authorZhang, Genen
dc.contributor.authorQian, Pei-Yuanen
dc.date.accessioned2014-11-11T14:31:08Z-
dc.date.available2014-11-11T14:31:08Z-
dc.date.issued2013-05-22en
dc.identifier.citationHe L-S, Zhang G, Qian P-Y (2013) Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite. PLoS ONE 8: e64130. doi:10.1371/journal.pone.0064130.en
dc.identifier.issn1932-6203en
dc.identifier.pmid23717550en
dc.identifier.doi10.1371/journal.pone.0064130en
dc.identifier.urihttp://hdl.handle.net/10754/334590en
dc.description.abstractThe 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. © 2013 He et al.en
dc.description.sponsorshipThe authors’ research grant from China Ocean Mineral Resources Research and Development Association (DY125-15-T-02), and King Abdullah University of Science and Technology (SA-C0040/UK-C0016) to P.Y. Qian. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en
dc.language.isoenen
dc.publisherPublic Library of Scienceen
dc.rightsThis 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 credited.en
dc.subject20k cement protein 1en
dc.subject20k cement protein 2en
dc.subjectcysteineen
dc.subjecthistidineen
dc.subjectproteinen
dc.subjectunclassified drugen
dc.subjectAmphibalanus amphitriteen
dc.subjectbarnacleen
dc.subjectdisulfide bonden
dc.subjectFistulobalanus albicostatusen
dc.subjectMegabalanus rosaen
dc.subjectnucleotide sequenceen
dc.subjectprotein analysisen
dc.subjectprotein domainen
dc.subjectprotein functionen
dc.subjectprotein localizationen
dc.subjectprotein structureen
dc.subjectsecretory cellen
dc.subjectsequence homologyen
dc.subjectAmino Acid Sequenceen
dc.subjectMolecular Sequence Dataen
dc.subjectPhylogenyen
dc.subjectProteinsen
dc.subjectSequence Homology, Amino Aciden
dc.subjectThoracicaen
dc.titleCharacterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitriteen
dc.typeArticleen
dc.identifier.journalPLoS ONEen
dc.identifier.pmcidPMC3661472en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionKAUST Global Collaborative Research Program, Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, Chinaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.grant.numberSA-C0040en
kaust.grant.numberUK-C0016en
kaust.grant.programKAUST Global Collaborative Research Programen

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.