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Molecules 2015, 20(2), 1788-1823; doi:10.3390/molecules20021788

Lectins: Getting Familiar with Translators of the Sugar Code

1
Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany
2
School of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland
*
Author to whom correspondence should be addressed.
Academic Editor: Tzi Bun NG
Received: 2 December 2014 / Revised: 23 December 2014 / Accepted: 8 January 2015 / Published: 22 January 2015
(This article belongs to the Special Issue Lectins)
View Full-Text   |   Download PDF [27563 KB, uploaded 22 January 2015]   |  

Abstract

The view on the significance of the presence of glycans in glycoconjugates is undergoing a paradigmatic change. Initially mostly considered to be rather inert and passive, the concept of the sugar code identifies glycans as highly versatile platform to store information. Their chemical properties endow carbohydrates to form oligomers with unsurpassed structural variability. Owing to their capacity to engage in hydrogen (and coordination) bonding and C-H/π-interactions these “code words” can be “read” (in Latin, legere) by specific receptors. A distinct class of carbohydrate-binding proteins are the lectins. More than a dozen protein folds have developed carbohydrate-binding capacity in vertebrates. Taking galectins as an example, distinct expression patterns are traced. The availability of labeled endogenous lectins facilitates monitoring of tissue reactivity, extending the scope of lectin histochemistry beyond that which traditionally involved plant lectins. Presentation of glycan and its cognate lectin can be orchestrated, making a glycan-based effector pathway in growth control of tumor and activated T cells possible. In order to unravel the structural basis of lectin specificity for particular glycoconjugates mimetics of branched glycans and programmable models of cell surfaces are being developed by strategic combination of lectin research with synthetic and supramolecular chemistry. View Full-Text
Keywords: adhesion; ganglioside; glycocluster; glycosylation; kidney; sialylation adhesion; ganglioside; glycocluster; glycosylation; kidney; sialylation
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

André, S.; Kaltner, H.; Manning, J.C.; Murphy, P.V.; Gabius, H.-J. Lectins: Getting Familiar with Translators of the Sugar Code. Molecules 2015, 20, 1788-1823.

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