Characterization of Two 20kDa-Cement Protein (cp20k) Homologues in Amphibalanus amphitrite
Permanent link to this recordhttp://hdl.handle.net/10754/334590
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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.
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.
SponsorsThe 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.
PublisherPublic Library of Science (PLoS)
PubMed Central IDPMC3661472
CollectionsPublications Acknowledging KAUST Support
- Toward understanding barnacle cementing by characterization of one cement protein-100kDa in Amphibalanus amphitrite.
- Authors: He LS, Zhang G, Wang Y, Yan GY, Qian PY
- Issue date: 2018 Jan 1
- Molt-dependent transcriptomic analysis of cement proteins in the barnacle Amphibalanus amphitrite.
- Authors: Wang Z, Leary DH, Liu J, Settlage RE, Fears KP, North SH, Mostaghim A, Essock-Burns T, Haynes SE, Wahl KJ, Spillmann CM
- Issue date: 2015 Oct 24
- Novel barnacle underwater adhesive protein is a charged amino acid-rich protein constituted by a Cys-rich repetitive sequence.
- Authors: Kamino K
- Issue date: 2001 Jun 1
- Calcite-specific coupling protein in barnacle underwater cement.
- Authors: Mori Y, Urushida Y, Nakano M, Uchiyama S, Kamino K
- Issue date: 2007 Dec
- Barnacle cement proteins. Importance of disulfide bonds in their insolubility.
- Authors: Kamino K, Inoue K, Maruyama T, Takamatsu N, Harayama S, Shizuri Y
- Issue date: 2000 Sep 1
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