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Glycobiology Advance Access originally published online on September 20, 2009
Glycobiology 2010 20(1):87-98; doi:10.1093/glycob/cwp151
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin

Emilie Lameignere2, Tze Chieh Shiao3, René Roy3, Michaela Wimmerova4, Fréderic Dubreuil2, Annabelle Varrot2 and Anne Imberty1,2

2 CERMAV-CNRS (affiliated with Université Joseph Fourier and belonging to ICMG), BP 53, F-38041, Grenoble, Cedex 09, France
3 Département de Chimie, Université du Québec à Montréal, B.P. 8888, Succ. Centre-Ville, Montréal (Québec), H3C 3P8, Canada
4 Department of Biochemistry and NCBR, Faculty of Science, Masaryk University, Kotlarska 2, 611 37 Brno, Czech Republic

1 To whom correspondence should be addressed: Tel: +33-4-76037636; Fax: +33-4-76547203; e-mail: anne.imberty{at}cermav.cnrs.fr

Received on July 27, 2009; revised on September 16, 2009; accepted on September 16, 2009

The opportunistic pathogen Burkholderia cenocepacia contains three soluble carbohydrate-binding proteins, related to the fucose-binding lectin PA-IIL from Pseudomonas aeruginosa. All contain a PA-IIL-like domain and two of them have an additional N-terminal domain that displays no sequence similarities with known proteins. Printed arrays screening performed on the shortest one, B. cenocepacia lectin A (BC2L-A), demonstrated the strict specificity for oligomannose-type N-glycan structures (Lameignere E, Malinovská L, Sláviková M, Duchaud E, Mitchell EP, Varrot A, Sedo O, Imberty A, Wimmerová M. 2008. Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia. Biochem J. 411:307–318.). The disaccharides {alpha}Man1-2Man, {alpha}Man1-3Man, and {alpha}Man1-6Man and the trisaccharide {alpha}Man1-3({alpha}Man1-6)Man were tested by titration microcalorimetry in order to evaluate their affinity for BC2L-A in solution and to characterize the thermodynamics of the binding. Oligomannose analogs presenting two mannoside residues separated by either flexible or rigid spacer were also tested. Only the rigid one yields to high affinity binding with a fast kinetics of clustering, while the flexible analog and the trimannoside display moderate affinities and no clustering effect on short time scale. The crystal structures of BC2L-A have been obtained in complex with {alpha}Man1-3Man disaccharide and {alpha}Man1({alpha}Man1-6)-3Man trisaccharide. The lengthy time required for the co-crystallization with the trisaccharide allowed for the formation of cluster since in the BC2L-A-trimannose complex solved at 1.1 Å resolution, the sugar creates a bridge between two adjacent dimers, yielding to molecular strings. AFM experiments were performed in order to visualize the filaments formed in solution by this type of interaction.

Key words: bacterial lectin / Burkholderia cenocepacia / mannose / oligosaccharides


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