期刊
HISTOCHEMISTRY AND CELL BIOLOGY
卷 147, 期 2, 页码 199-222出版社
SPRINGER
DOI: 10.1007/s00418-016-1524-6
关键词
Agglutinin; Glycoprotein; Glycosylation; Protein fold; Sialylation
资金
- excellence program of the Ludwig-Maximilians-University Munich
- Verein zur Forderung des bio-logischtechnologischen Fortschritts in der Medizin e.V. (Heidelberg, Germany)
- EC (for ITN network)
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.
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