Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries
Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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.
Original language | English |
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Title of host publication | Galectins : Methods and Protocols |
Number of pages | 10 |
Publisher | Humana Press |
Publication date | 2022 |
Pages | 205-214 |
ISBN (Print) | 978-1-0716-2054-0 |
ISBN (Electronic) | 978-1-0716-2055-7 |
DOIs | |
Publication status | Published - 2022 |
Series | Methods in Molecular Biology |
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Volume | 2442 |
ISSN | 1064-3745 |
Bibliographical note
Publisher Copyright:
© 2022, Springer Science+Business Media, LLC, part of Springer Nature.
- Carbohydrate binding proteins, Galectin, Gene editing, Glycoengineering, Glycogenes, Glycosylation, Glycosyltransferases, Substrate specificity
Research areas
ID: 305715154