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Structural characterisation of the N-glycan moiety of the barnacle settlement-inducing protein complex (SIPC)

Lookup NU author(s): Helen Pagett, Dr Jon Marles-WrightORCiD, Professor Rick Lewis, Professor Robin Harris, Dr Gary Caldwell, Professor Tony Clare

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Abstract

Many 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.


Publication metadata

Author(s): Pagett HE, Abrahams JL, Bones J, O'Donoghue N, Marles-Wright J, Lewis RJ, Harris JR, Caldwell GS, Rudd PM, Clare AS

Publication type: Article

Publication status: Published

Journal: Journal of Experimental Biology

Year: 2012

Volume: 215

Issue: 7

Pages: 1192-1198

Print publication date: 01/04/2012

ISSN (print): 0022-0949

ISSN (electronic): 1477-9145

Publisher: The Company of Biologists Ltd.

URL: http://dx.doi.org/10.1242/jeb.063503

DOI: 10.1242/jeb.063503


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Funding

Funder referenceFunder name
037661EU
NER/S/A/2007/14628National Environment Research Council

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