Lectins: a primer for histochemists and cell biologists

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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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    Such an apparent lack of enthusiasm in an early phase of study allows to draw an analogy to the course of development similarly encountered in the case of nuclein (first isolated in 1869, renamed to nucleic acid in 1889) (Chargaff 1970; Dahm 2005). Following nuclein’s biochemical characterization, “then the long road began—in this case nearly 80 years—which every biologically important, complicated chemical substance must travel: first its structure, then its function” (Chargaff 1977). Accompanied by encouraging statements such as that lectins “promise to have theoretical and practical importance” (Boyd and Shapleigh 1954), the topic of an “obscure” research field eventually made it into the “limelight” (Sharon 1998). Breaking the sugar code and “identifying the receptors,” then analyzing the functional pairing of lectin and its counterreceptor(s) “are of prime importance” (Sharon 1998), long-range aims that sparked vigorous research activity, for example by using ConA as research tool (Bittiger and Schnebli 1976).


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We gratefully acknowledge inspiring discussions with Drs. B. Friday, C. Knospe, A. Leddoz and F. Sinowatz as well as generous funding by the excellence program of the Ludwig-Maximilians-University Munich, the Verein zur Förderung des biologisch-technologischen Fortschritts in der Medizin e.V. (Heidelberg, Germany) and the EC (for ITN network funding; GLYCOPHARM).

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Correspondence to Hans-Joachim Gabius.

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Joachim C. Manning, Antonio Romero and Felix A. Habermann have contributed equally to this work.

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Manning, J.C., Romero, A., Habermann, F.A. et al. Lectins: a primer for histochemists and cell biologists. Histochem Cell Biol 147, 199–222 (2017) doi:10.1007/s00418-016-1524-6

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  • Agglutinin
  • Glycoprotein
  • Glycosylation
  • Protein fold
  • Sialylation