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Glycobiology Advance Access published online on April 6, 2009
Glycobiology, doi:10.1093/glycob/cwp049
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Analysis of lectin binding to glycolipid complexes using combinatorial glycoarrays

Simon Rinaldi1, Kathryn M. Brennan1, Carl S. Goodyear1, Colin O’Leary1, Giampietro Schiavo2, Paul R. Crocker3 and Hugh J. Willison1

1 Division of Clinical Neurosciences, Glasgow Biomedical Research Centre, University of Glasgow, Glasgow G12 8TA, United Kingdom
2 Molecular NeuroPathobiology Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK
3 Wellcome Trust Biocentre, University of Dundee, Dow Street, Dundee DD1 5EH (UK)

Address for correspondence: Professor Hugh J. Willison, Glasgow Biomedical Research Centre, Room B330, 120 University Place, University of Glasgow, Glasgow G12 8TA, Tel: 44 (0) 141 330 8384, Fax: 44 (0) 141 201 2993, e-mail: h.j.willison{at}clinmed.gla.ac.uk

Received on February 18, 2009; accepted on March 31, 2009

Glycolipids are major components of the plasma membrane, interacting with themselves, other lipids and proteins to form an array of heterogeneous domains with diverse biological properties. Considerable effort has focused on identifying protein binding partners for glycolipids and the glycan specificity for these interactions, largely achieved through assessing interactions between proteins and homogenous, single species glycolipid preparations. This approach risks overlooking both the enhancing and attenuating role of heterogeneous glycolipid complexes in modulating lectin binding. Here we report a simple method for assessing lectin-glycolipid interactions. An automatic thin layer chromatography sampler is employed to create easily reproducible arrays of glycolipids and their heterodimeric complexes immobilized on a synthetic polyvinyl-difluoride membrane. This array can then be probed with much smaller quantities of reagents than would be required using existing techniques such as ELISA and thin-layer chromatography with immuno-overlay. Using this protocol, we have established that the binding of bacterial toxins, lectins, and antibodies can each be attenuated, enhanced or unaffected in the presence of glycolipid complexes, as compared with individual, isolated glycolipids. These findings underpin the wide-ranging influence and importance of glycolipid-glycolipid cis interactions when the nature of protein-carbohydrate recognition events are being assessed.

Key words: complexes / ganglioside / glycoarray / glycolipid / lectin


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