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dc.contributor.authorPagett, Helen E.
dc.contributor.authorAbrahams, Jodie L.
dc.contributor.authorBones, Jonathan
dc.contributor.authorO'Donoghue, Niaobh
dc.contributor.authorMarles-Wright, Jon
dc.contributor.authorLewis, Richard J.
dc.contributor.authorHarris, J. Robin
dc.contributor.authorCaldwell, Gary S.
dc.contributor.authorRudd, Pauline M.
dc.contributor.authorClare, Anthony S.
dc.date.accessioned2017-08-11T03:31:43Z
dc.date.available2017-08-11T03:31:43Z
dc.date.issued2012
dc.identifier.issn1477-9145
dc.identifier.doi10.1242/jeb.063503
dc.identifier.urihttp://hdl.handle.net/10072/343822
dc.description.abstractMany barnacle species are gregarious and their cypris larvae display a remarkable ability to explore surfaces before committing to permanent attachment. The chemical cue to gregarious settlement behaviour – the settlement-inducing protein complex (SIPC) – is an α2-macroglobulin-like glycoprotein. This cuticular protein may also be involved in cyprid reversible adhesion if its presence is confirmed in footprints of adhesive deposited during exploratory behaviour, which increase the attractiveness of surfaces and signal other cyprids to settle. The full-length open-reading frame of the SIPC gene encodes a protein of 1547 amino acids with seven potential N-glycosylation sites. In this study on Balanus amphitrite, glycan profiling of the SIPC via hydrophilic interaction liquid chromatography with fluorescence detection (HILIC-fluorescence) provided evidence of predominantly high mannose glycans (M2–9), with the occurrence of monofucosylated oligomannose glycans (F(6)M2–4) in lower proportions. The high mannose glycosylation found supports previous observations of an interaction with mannose-binding lectins and exogenous mannose increasing settlement in B. amphitrite cypris larvae. Transmission electron microscopy of the deglycosylated SIPC revealed a multi-lobed globular protein with a diameter of ∼8 nm. Obtaining a complete structural characterisation of the SIPC remains a goal that has the potential to inspire solutions to the age-old problem of barnacle fouling.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherThe Company of Biologists
dc.relation.ispartofpagefrom1192
dc.relation.ispartofpageto1198
dc.relation.ispartofissue7
dc.relation.ispartofjournalJournal of Experimental Biology
dc.relation.ispartofvolume215
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode060199
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.titleStructural characterisation of the N-glycan moiety of the barnacle settlement-inducing protein complex (SIPC)
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyrightSelf-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the author[s] for more information.
gro.hasfulltextNo Full Text
gro.griffith.authorAbrahams, Jodie L.


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