Lectins: a primer for histochemists and cell biologists
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.
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Plant and animal lectins are a class of carbohydrate-binding proteins distinct from antibodies, enzymes, and transport proteins for free mono-, di-, and oligosaccharides.
“Plant and animal lectins are a class of carbohydrate-binding proteins distinct from antibodies, enzymes and transport proteins for free mono-, di- and oligosaccharides (for details on definition and applications, see Manning et al. 2017).”
From An introduction to the sugar code (2017) · cites this paper as Manning et al. 2017
The existence of more than a dozen folds for lectins attests that glycan diversity is matched on the level of lectins.
“The existence of more than a dozen folds for proteins falling into this category attests that diversity of glycans is matched on the level of lectins [see Galleries of Lectins for animal and human lectins in Solís et al. (2015) and for plant and fungal lectins in Manning et al. (2017)].”
From An introduction to the sugar code (2017) · cites this paper as Manning et al. 2017
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References 106 · Cited by 133
- Authors
- Manning, J. C., Romero, A., Habermann, F. A., García Caballero, G., Kaltner, H., & Gabius, H.-J.
- Affiliations
- Ludwig-Maximilians-Universität München (DE)
- Consejo Superior de Investigaciones Científicas (ES)
- Anatomische Anstalt (DE)
- Corresponding author
- Gabius, Hans-Joachim
- Venue
- Histochemistry and Cell Biology
- Published
- 2016-12-24
- Volume
- 147
- Issue
- 2
- Pages
- 199-222
- ISSN
- 0948-6143 (ISSN-L)
- 1432-119X
- OpenAlex
- W2565754182
- Cited by
- 133
- References
- 106
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 13 · 2021: 14 · 2020: 16 · 2019: 21 · 2018: 20 · 2017: 16 · 2016: 8
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Histochemistry and Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- lectins, glycan-binding proteins, glycoconjugates, carbohydrate receptors, hemagglutination, blood group antigens, plant lectins, fungal lectin, lectin structure, cell adhesion, host defense, lectin histochemistry
- MeSH terms
- Animals, Cell Biology, Glycosylation, Humans, Protein Folding, Lectins
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