Not to be confused with Leptin or Lecithin.
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]
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Contents
- 1 Etymology
- 2 History
- 3 Biological functions
- 3.1 Functions in animals
- 3.2 Functions in plants
- 4 Use in science, medicine and technology
- 4.1 Use in medicine and medical research
- 4.2 Use in studying carbohydrate recognition by proteins
- 4.3 Use as a biochemical tool
- 4.4 Use in biochemical warfare
- 5 Toxicity
- 5.1 Digestion and immune distress
- 5.2 Lectin and Leptin Resistance
- 6 See also
- 7 References
- 8 Further reading
- 9 External links
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Etymology
| 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
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,
R2-GlcNAcβ1-4(Fucα1-6)GlcNAc-R1
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The name "lectin" is derived from the Latin word legere, meaning, among other things, "to select".(lek'tin)
History
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.
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
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.[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.[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.[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 as well as in microarrays as in evanescent-field fluorescence-assisted lectin microarray.[8]
Use in biochemical warfare
One example of the powerful biological attributes of lectins is the biochemical warfare agent ricin. The protein ricin is isolated from seeds of the castor oil plant and comprises two protein domains. Abrin from the jequirity pea is similar:
- One domain 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.
Toxicity
Digestion and immune distress
Foods with high concentrations of lectins, such as beans, cereal grains, seeds, nuts, and potatoes, may be harmful if consumed in excess in uncooked or improperly cooked form. Adverse effects may include nutritional deficiencies, and immune (allergic) reactions.[9] 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.[10]
For various reasons foods have been genetically modified with lectins, such as potatoes containing the GNA gene from the snowdrop plant.[citation needed] In 1998 Árpád Pusztai said in an interview on a World in Action programme that his group had observed damage to the intestines and immune systems of rats fed the genetically modified potatoes. He also said "If I had the choice I would certainly not eat it", and that "I find it's very unfair to use our fellow citizens as guinea pigs".[11] These remarks started the Pusztai affair.
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.[12] Such leptin resistance may translate into diseases, notably it could be responsible for obesity in humans who have high levels of leptin.
See also
- Concanavalin A, Phytohaemagglutinin
- Con A Proteopedia 1bxh, Pokeweed lectin Proteopedia 1uha, Artocarpus lectin Proteopedia 1toq, Pterocarpus lectin Proteopedia 1q8v, Urtica lectin Proteopedia 1en2
- Toxalbumin
References
- ^ http://www.krispin.com/lectin.html
- ^ "Lectin list". Interchim. 2010. http://www.interchim.fr/ft/M/MS902z.pdf. Retrieved 2010-05-05.
- ^ Komath SS, Kavitha M, Swamy MJ (March 2006). "Beyond carbohydrate binding: new directions in plant lectin research". Org. Biomol. Chem. 4 (6): 973–88. doi:10.1039/b515446d. PMID 16525538.
- ^ The History of Lectins by N.Sharon
- ^ Carlson, Neil R. (2007). Physiology of behavior. Boston: Pearson Allyn & Bacon. ISBN 0-205-46724-5.
- ^ http://www.jbc.org/content/285/12/8646.abstract "A Lectin Isolated from Bananas Is a Potent Inhibitor of HIV Replication" 2010
- ^ [1]
- ^ Glyco Station, Lec Chip, Glycan profiling technology
- ^ British Journal of Nutrition (2000), 83: 207-217 Cambridge University Press
- ^ Miyake K, Tanaka T, McNeil PL (2007). Steinhardt, Richard. ed. "Lectin-Based Food Poisoning: A New Mechanism of Protein Toxicity". PLoS ONE 2 (1): e687. doi:10.1371/journal.pone.0000687. PMC 1933252. PMID 17668065. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1933252/.
- ^ "Árpád Pusztai: Biological Divide – James Randerson interviews biologist Árpád Pusztai". London: The Guardian. 15 January 2008. http://education.guardian.co.uk/egweekly/story/0,,2240547,00.html. Retrieved 25 April 2010.
- ^ 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
- Halina Lis; Sharon, Nathan (2007). Lectins (Second ed.). Berlin: Springer. ISBN 1-4020-6605-8.
- Ni Y, Tizard I (1996). "Lectin-carbohydrate interaction in the immune system". Vet Immunol Immunopathol 55 (1–3): 205–23. doi:10.1016/S0165-2427(96)05718-2. PMID 9014318.
External links
- Functional Glycomics Gateway, a collaboration between the Consortium for Functional Glycomics and Nature Publishing Group
- Introduction by Jun Hirabayashi
- Proteopedia shows more than 800 three-dimensional molecular models of lectins, fragments of lectins and complexes with carbohydrates
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Protein: lectins
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| Animal |
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C-type lectins
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- Asialoglycoprotein receptor
- KLRD1
- Collectin
- Mannose receptor
- proteochondroitin sulfate
- Aggrecan
- Versican
- Brevican
- Neurocan
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Other
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- Calnexin
- Calreticulin
- CD22
- CD33
- Galectin
- Myelin-associated glycoprotein
- N-Acetylglucosamine receptor
- Selectin
- Sialoadhesin
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| Plant |
- Abrin
- Ricin
- Mitogens
- Concanavalin A
- Phytohaemagglutinin
- Pokeweed mitogen
- Legume lectin
- BanLec
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