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File:Hemagglutinin lateral.jpg
Lateral hemagglutinine

Lectins are sugar-binding proteins (not to be confused with glycoproteins, which are proteins containing sugar chains or residues) that are highly specific for their sugar moieties. They play a role in biological recognition phenomena involving cells and proteins. For example, some viruses use lectins to attach themselves to the cells of the host organism during infection. Lectins may be disabled by specific mono- and oligosaccharides, which bind to them and prevent their attachment to cell membranes.[1]


Table of the major lectins [2]
  Lectin Symbol Lectin name Source ligand motif
Mannose binding lectins
ConA Concanavalin A Canavalia ensiformis α-D-mannosyl and α-D-glucosyl residues </br>

branched α-mannosidic structures (high α-mannose type, or hybrid type and biantennary complex type N-Glycans)

LCH Lentil lectin Lens culinaris Fucosylated core region of bi- and triantennary complex type N-Glycans
GNA Snowdrop lectin Galanthus nivalis α 1-3 and α 1-6 linked high mannose structures
Galactose / N-acetylgalactosamine binding lectins
RCA Ricin, Ricinus communis Agglutinin, RCA120 Ricinus communis Galβ1-4GlcNAcβ1-R
PNA Peanut agglutinin Arachis hypogaea Galβ1-3GalNAcα1-Ser/Thr (T-Antigen)
AIL Jacalin Artocarpus integrifolia (Sia)Galβ1-3GalNAcα1-Ser/Thr (T-Antigen)
VVL Hairy vetch lectin Vicia villosa GalNAcα-Ser/Thr (Tn-Antigen)
N-acetylglucosamine binding lectins
WGA Wheat Germ Agglutinin, WGA Triticum vulgaris GlcNAcβ1-4GlcNAcβ1-4GlcNAc, Neu5Ac (sialic acid)
N-acetylneuraminic acid binding lectins
SNA Elderberry lectin Sambucus nigra Neu5Acα2-6Gal(NAc)-R
MAL Maackia amurensis leukoagglutinin Maackia amurensis Neu5Ac/Gcα2,3Galβ1,4Glc(NAc)
MAH Maackia amurensis hemoagglutinin Maackia amurensis Neu5Ac/Gcα2,3Galβ1,3(Neu5Acα2,6)GalNac
Fucose binding lectins
UEA Ulex europaeus agglutinin Ulex europaeus Fucα1-2Gal-R
AAL Aleuria aurantia lectin Aleuria aurantia Fucα1-2Galβ1-4(Fucα1-3/4)Galβ1-4GlcNAc, </br>


The name "lectin" is derived from the Latin word legere, meaning, among other things, "to select".(lek'tin)


Although they were first discovered more than 100 years ago in plants, they are now known to be present throughout nature. It is generally believed that the earliest description of a lectin was given by Peter Hermann Stillmark in his doctoral thesis presented in 1888 to the University of Dorpat. Stillmark isolated ricin, an extremely toxic hemagglutinin, from seeds of the castor plant (Ricinus communis) The first lectin to be purified on a large scale and available on a commercial basis was concanavalin A, which is now the most-used lectin for characterization and purification of sugar-containing molecules and cellular structures. The legume lectins are probably the most well-studied lectins.

Biological functions

Most lectins are non-enzymatic in action and non-immune in origin. Lectins occur ubiquitously in nature. They may bind to a soluble carbohydrate or to a carbohydrate moiety that is a part of a glycoprotein or glycolipid. They typically agglutinate certain animal cells and/or precipitate glycoconjugates.

File:Gs4 sugar all.png
An oligosaccharide (shown in grey) bound in the binding site of a plant lectin (Griffonia simplicifolia isolectin IV in complex with the Lewis b blood group determinant). Only a part of the oligosaccharide (central, in grey) is shown for clarity.

Functions in animals

Lectins serve many different biological functions in animals, from the regulation of cell adhesion to glycoprotein synthesis and the control of protein levels in the blood. They may also bind soluble extracellular and intercellular glycoproteins. Some lectins are found on the surface of mammalian liver cells that specifically recognize galactose residues. It is believed that these cell-surface receptors are responsible for the removal of certain glycoproteins from the circulatory system. Another lectin is a receptor that recognizes hydrolytic enzymes containing mannose-6-phosphate, and targets these proteins for delivery to the lysosomes. I-cell disease is one type of defect in this particular system. Lectins are also known to play important roles in the immune system by recognizing carbohydrates that are found exclusively on pathogens, or that are inaccessible on host cells. Examples are the lectin complement activation pathway and mannose-binding lectin.

Functions in plants

File:Phytohemagglutinin L.png
Leucoagglutinin, a toxic phytohemagglutinin found in raw Vicia faba

The function of lectins in plants (legume lectin) is still uncertain. Once thought to be necessary for rhizobia binding, this proposed function was ruled out through lectin-knockout transgene studies.Template:Citation needed

The large concentration of lectins in plant seeds decreases with growth, and suggests a role in plant germination and perhaps in the seed's survival itself. The binding of glycoproteins on the surface of parasitic cells is also believed to be a function. Several plant lectins have been found to recognise non-carbohydrate ligands that are primarily hydrophobic in nature, including adenine, auxins, cytokinin, and indole acetic acid, as well as water-soluble porphyrins. It has been suggested that these interactions may be physiologically relevant, since some of these molecules function as phytohormones.[3] are another major family of protein ANCs, which are specific sugar-binding proteins exhibiting reversible carbohydrate-binding activities. Lectins are similar to antibodies in their ability to agglutinate red blood cells; however, lectins are not the product of immune system. The toxicity of lectins has been identified by consumption of food with high content of lectins, which can lead to diarrhea, nausea, bloating, vomiting, even death (as from ricin). Many legume seeds have been proven to contain high lectin activity, termed as hemagglutinating activity. Soybean is the most important grain legume crop, the seeds of which contain high activity of soybean lectins (soybean agglutinin or SBA). SBA is able to disrupt small intestinal metabolism and damage small intestinal villi via the ability of lectins to bind with brush border surfaces in the distal part of small intestine.Template:Citation needed Heat processing can reduce the toxicity of lectins, but low temperature or insufficient cooking may not completely eliminate their toxicity, as some plant lectins are resistant to heat. (It is believed that undercooking red kidney beans increases toxicity.) In addition, lectins can result in irritation and over-secretion of mucus in the intestines, causing impaired absorptive capacity of the intestinal wall.Template:Citation needed

Use in science, medicine and technology

Use in medicine and medical research

Purified lectins are important in a clinical setting because they are used for blood typing.[4] Some of the glycolipids and glycoproteins on an individual's red blood cells can be identified by lectins.

  • A lectin from Dolichos biflorus is used to identify cells that belong to the A1 blood group.
  • A lectin from Ulex europaeus is used to identify the H blood group antigen.
  • A lectin from Vicia graminea is used to identify the N blood group antigen.
  • A lectin from " Coconut milk" is used to identify Theros antigen.
  • A lectin from "Dorex is used to identify R antigen.

In neuroscience, the anterograde labeling method is used to trace the path of efferent axons with PHA-L, a lectin from the kidney bean.[5]

A lectin (BanLec) from bananas inhibits HIV-1 in vitro[6]

Use in studying carbohydrate recognition by proteins

Lectins from legume plants, such as PHA or concanavalin A, have been widely used as model systems to understand the molecular basis of how proteins recognize carbohydrates, because they are relatively easy to obtain and have a wide variety of sugar specificities. The many crystal structures of legume lectins have led to a detailed insight of the atomic interactions between carbohydrates and proteins.

Use as a biochemical tool

Concanavalin A and other commercially available lectins have been widely used in affinity chromatography for purifying glyco proteins.[7]

In general, proteins may be characterized with respect to glycoforms and carbohydrate structure by means of affinity chromatography, blotting, affinity electrophoresis and affinity immunoelectrophoreis with lectins.

Use in biochemical warfare

One example of the powerful biological attributes of lectins is the biochemical warfare agent ricin. Ricin is isolated from seeds of the castor oil plant and is a protein that comprises two domains. Abrin from the jequirity pea is similar:

  • One is a lectin that binds cell surface galactosyl residues and enables the protein to enter cells
  • The second domain is an N-glycosidase that cleaves nucleobases from ribosomal RNA, resulting in inhibition of protein synthesis and cell death.


Digestion and immune distress

Foods with high concentrations of lectins, such as beans, cereal grains, seeds, and nuts, may be harmful if consumed in excess in uncooked or improperly cooked form. Adverse effects may include nutritional deficiencies, and immune (allergic) reactions.[8] Possibly, most effects of lectins are due to gastrointestinal distress through interaction of the lectins with the gut epithelial cells. A recent in vitro study has suggested that the mechanism of lectin damage may occur by interfering with the repair of already-damaged epithelial cells.[9]

Lectin and Leptin Resistance

Lectin may cause leptin resistance, affecting its functions (signal have high levels of leptin and several effects gathering to protect from lipid overload), as indicated by studies on effects of single nucleotide polymorphisms on the function of leptin and the leptin receptor.[10] Such leptin resistance may translate into diseases, notably it could be responsible for obesity in humans who have high levels of leptin.

See also



  1. http://www.krispin.com/lectin.html
  2. http://en.wikipedia.org/wiki/Oil-drop_experiment
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  4. The History of Lectins by N.Sharon
  5. Template:Cite book
  6. http://www.jbc.org/content/285/12/8646.abstract "A Lectin Isolated from Bananas Is a Potent Inhibitor of HIV Replication" 2010
  7. GE Healthcare Life Sciences, Immobilized lectin
  8. British Journal of Nutrition (2000), 83: 207-217 Cambridge University Press
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  10. T Jönsson, S Olsson, B Ahrén , T C Bøg-Hansen, A Dole and S Lindeberg (2005). "Agrarian diet and diseases of affluence – Do evolutionary novel dietary lectins cause leptin resistance?". BioMed Central Ltd.. doi:10.1186/1472-6823-5-10. . http://www.biomedcentral.com/1472-6823/5/10.

Further reading


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External links

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