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Published online 17 May 2004. doi:10.1083/jcb.200309005
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 4, 529-537
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Article

 Carbohydrate–carbohydrate interaction provides adhesion force and specificity for cellular recognition

Iwona Bucior1,2, Simon Scheuring3, Andreas Engel3, and Max M. Burger1,2

1 Friedrich Miescher Institute, 4058 Basel, Switzerland
2 Marine Biological Laboratories, Woods Hole, MA 02543
3 M.E. Müller Institute for Microscopy, Biozentrum, University of Basel, 4056 Basel, Switzerland

Address correspondence to Max M. Burger, Novartis Science Board, Novartis International AG, WKL-125.13.02, CH-4002 Basel, Switzerland. Tel: 41-61-696-7690. Fax: 41-61-696-7693. email: max.burger{at}group.novartis.com

The adhesion force and specificity in the first experimental evidence for cell–cell recognition in the animal kingdom were assigned to marine sponge cell surface proteoglycans. However, the question whether the specificity resided in a protein or carbohydrate moiety could not yet be resolved. Here, the strength and species specificity of cell–cell recognition could be assigned to a direct carbohydrate–carbohydrate interaction. Atomic force microscopy measurements revealed equally strong adhesion forces between glycan molecules (190–310 piconewtons) as between proteins in antibody–antigen interactions (244 piconewtons). Quantitative measurements of adhesion forces between glycans from identical species versus glycans from different species confirmed the species specificity of the interaction. Glycan-coated beads aggregated according to their species of origin, i.e., the same way as live sponge cells did. Live cells also demonstrated species selective binding to glycans coated on surfaces. These findings confirm for the first time the existence of relatively strong and species-specific recognition between surface glycans, a process that may have significant implications in cellular recognition.

Key Words: cell–cell recognition; cell surface proteoglycan; carbohydrate–carbohydrate interaction; species specificity; adhesion force

S. Scheuring's present address is Institut Curie, UMR-CNRS 168, LRC-CEA 8, 11 rue Pierre et Marie Curie, 75231 Paris, Cedex 05, France.

Abbreviations used in this paper: AFM, atomic force microscopy; CSW, Ca2+- and Mg2+-free artificial seawater buffered with 20 mM Tris, pH 7.4, supplemented with 2 mM CaCl2; Lex, Lewisx determinant (Galß1->4[Fuc{alpha}1->3]GlcNAcß1->3Galß1->4Glcß); pN, piconewtons.


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