Abstract
An experimental observation on selecting binding partners underlies the introduction of the term ‘lectin’. Agglutination of erythrocytes depending on their blood-group status revealed the presence of activities in plant extracts that act in an epitope-specific manner like antibodies. As it turned out, their binding partners on the cell surface are carbohydrates of glycoconjugates. By definition, lectins are glycan-specific (mono- or oligosaccharides presented by glycoconjugates or polysaccharides) receptors, distinguished from antibodies, from enzymes using carbohydrates as substrates and from transporters of free saccharides. They are ubiquitous in Nature and structurally widely diversified. More than a dozen types of folding pattern have evolved for proteins that bind glycans. Used as tool, this capacity facilitates versatile mapping of glycan presence so that plant/fungal and also animal/human lectins have found a broad spectrum of biomedical applications. The functional pairing with physiological counterreceptors is involved in a wide range of cellular activities from cell adhesion, glycoconjugate trafficking to growth regulation and lets lectins act as sensors/effectors in host defense.
| Item Type: | Journal article |
|---|---|
| Form of publication: | Publisher's Version |
| Keywords: | Agglutinin; Glycoprotein; Glycosylation; Protein fold; Sialylation |
| Faculties: | Veterinary Medicine Veterinary Medicine > Department of Veterinary Medicine Veterinary Medicine > Department of Veterinary Medicine > Lehrstuhl für Anatomie, Histologie und Embryologie Veterinary Medicine > Department of Veterinary Medicine > Lehrstuhl für Physiologische Chemie |
| Subjects: | 500 Science > 500 Science 500 Science > 540 Chemistry 600 Technology > 610 Medicine and health |
| ISSN: | 0948-6143 |
| Language: | English |
| Item ID: | 36776 |
| Date Deposited: | 03. Apr 2017, 13:25 |
| Last Modified: | 04. Nov 2020, 13:14 |
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