Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries.

Methods Mol Biol

Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, Copenhagen Center for Glycomics, University of Copenhagen, Copenhagen, Denmark.

Published: March 2022

AI Article Synopsis

  • * Understanding galectin functions requires analyzing the binding preferences of their carbohydrate recognition domains (CRDs), which was traditionally done using glycoarrays.
  • * To study these binding specificities more effectively, researchers now use glycoengineered cell libraries that mimic natural cellular surfaces, along with fluorescence anisotropy to measure bindings in solution.

Article Abstract

The family of galectins has critical functions in a wide range of biological processes, primarily based on their broad interactions with proteins carrying β-galactoside-containing glycans. To understand the diversity of functions governed by galectins, it is essential to define the binding specificity of the carbohydrate recognition domain (CRDs) of the individual galectins. The binding specificity of galectins has primarily been examined with glycoarrays, but now the ability to probe and dissect binding to defined glycans in the context of a cellular membrane is facilitated by the generations of glycoengineered cell libraries with defined glyco-phenotypes. The following section will show how galectin specificities can be probed in the natural context of cellular surfaces using glycoengineered cell libraries, and how binding to glycoproteins can be measured in solution with fluorescence anisotropy.

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Source
http://dx.doi.org/10.1007/978-1-0716-2055-7_12DOI Listing

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