Dissecting the specificity of sugar code recognition - Unleashing the biomedical potential of galectins by protein engineering.
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| Title: | Dissecting the specificity of sugar code recognition - Unleashing the biomedical potential of galectins by protein engineering. |
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| Authors: | Kalka M; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Ptak J; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Gregorczyk P; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Ciura K; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Chorążewska A; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Haldar S; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Porębska N; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Marcinkowska E; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland., Opaliński Ł; Department of Medical Biotechnology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland. Electronic address: lukasz.opalinski@uwr.edu.pl. |
| Source: | Biotechnology advances [Biotechnol Adv] 2025 Nov; Vol. 84, pp. 108681. Date of Electronic Publication: 2025 Aug 05. |
| Publication Type: | Journal Article; Review |
| Language: | English |
| Journal Info: | Publisher: Elsevier Science Country of Publication: England NLM ID: 8403708 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-1899 (Electronic) Linking ISSN: 07349750 NLM ISO Abbreviation: Biotechnol Adv Subsets: MEDLINE |
| Imprint Name(s): | Publication: Oxford : Elsevier Science Original Publication: Oxford ; New York : Pergamon Press, c1983- |
| MeSH Terms: | Galectins*/chemistry , Galectins*/metabolism , Galectins*/genetics , Protein Engineering*/methods , Sugars*/metabolism , Sugars*/chemistry, Humans ; Animals |
| Abstract: | The cell surface is extremely rich in multilayered information that exists in the form of complex monosaccharide assemblies, establishing a cellular sugar code. The sugar code is specifically deciphered by extracellular lectins, galectins, which are capable of recognizing sugar code components and transforming the code into precise cellular activities. Galectin-dependent reading of the sugar code relies on two major features: the specific recognition of sugars by the galectins' carbohydrate recognition domains (CRDs) and the modular architecture of galectins or their oligomerization. These two characteristics of galectins are essential for most of galectins' functions, as they ensure the specificity of sugar code recognition and permit multivalent interactions with carbohydrate ligands. The natural galectins are characterized by relatively fixed modular architecture, which allows for evolutionarily defined reading of the sugar code, limiting the spectrum of biological activities of galectins. Distinct protein engineering approaches, like linker modulation, crosslinking, domain swapping or fusion with oligomerization scaffolds allow for the modulation of galectin multivalency in order to overcome the natural decoding limitations of galectins and permit alternative reading of the sugar code. In this review, we we provide an overview of the architectures of engineered galectins with altered valency and discuss how alternative reading of the code by such proteins may prove beneficial in biotechnology. (Copyright © 2025 The Author(s). Published by Elsevier Inc. All rights reserved.) |
| Competing Interests: | Declaration of competing interest The authors declare no conflict of interest. |
| Contributed Indexing: | Keywords: Affinity; Endocytosis; Galectin; Glycosylation; Oligomerization; Protein engineering; Protein scaffolds; Signaling; Sugar code; Valence |
| Substance Nomenclature: | 0 (Galectins) 0 (Sugars) |
| Entry Date(s): | Date Created: 20250807 Date Completed: 20250910 Latest Revision: 20250910 |
| Update Code: | 20250911 |
| DOI: | 10.1016/j.biotechadv.2025.108681 |
| PMID: | 40774568 |
| Database: | MEDLINE |
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