Lectin

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Lateral hemagglutinine Hemagglutinin lateral.jpg
Lateral hemagglutinine

Lectins are carbohydrate-binding proteins that are highly specific for sugar groups that are part of other molecules, so cause agglutination of particular cells or precipitation of glycoconjugates and polysaccharides. Lectins have a role in recognition at the cellular and molecular level and play numerous roles in biological recognition phenomena involving cells, carbohydrates, and proteins. [1] [2] Lectins also mediate attachment and binding of bacteria, viruses, and fungi to their intended targets.

Contents

Lectins are found in many foods. Some foods, such as beans and grains, need to be cooked, fermented or sprouted to reduce lectin content. Some lectins are beneficial, such as CLEC11A, which promotes bone growth, while others may be powerful toxins such as ricin. [3]

Lectins may be disabled by specific mono- and oligosaccharides, which bind to ingested lectins from grains, legumes, nightshade plants, and dairy; binding can prevent their attachment to the carbohydrates within the cell membrane. The selectivity of lectins means that they are useful for analyzing blood type, and they have been researched for potential use in genetically engineered crops to transfer pest resistance.

Etymology

Table of the major plant lectins [4]
  Lectin SymbolLectin nameSourceLigand 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)

LCHLentil lectin Lens culinaris Fucosylated core region of bi- and triantennary complex type N-Glycans
GNASnowdrop 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 Galβ1-4GalNAcβ1-R
PNA Peanut agglutinin Arachis hypogaea Galβ1-3GalNAcα1-Ser/Thr (T-Antigen)
AIL Jacalin Artocarpus integrifolius (Sia)Galβ1-3GalNAcα1-Ser/Thr (T-Antigen)
VVLHairy vetch lectin Vicia villosa GalNAcα-Ser/Thr (Tn-Antigen)
N-acetylglucosamine binding lectins
WGA Wheat germ agglutinin Triticum vulgaris GlcNAcβ1-4GlcNAcβ1-4GlcNAc, Neu5Ac (sialic acid)
N-acetylneuraminic acid binding lectins
SNA Elderberry lectin Sambucus nigra Neu5Acα2-6Gal(NAc)-R
MALMaackia amurensis leukoagglutinin Maackia amurensis Neu5Ac/Gcα2,3Galβ1,4Glc(NAc)
MAHMaackia amurensis hemoagglutininMaackia amurensisNeu5Ac/Gcα2,3Galβ1,3(Neu5Acα2,6)GalNac
Fucose binding lectins
UEAUlex europaeus agglutinin Ulex europaeus Fucα1-2Gal-R
AALAleuria aurantia lectin Aleuria aurantia Fucα1-2Galβ1-4(Fucα1-3/4)Galβ1-4GlcNAc,

R2-GlcNAcβ1-4(Fucα1-6)GlcNAc-R1

William C. Boyd alone and then together with Elizabeth Shapleigh [5] introduced the term "lectin" in 1954 from the Latin word lectus, "chosen" (from the verb legere, to choose or pick out). [6]

Biological functions

Lectins 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. Most lectins do not possess enzymatic activity.

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. 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.

Animals

Lectins have these functions in animals:

Plants

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. [9]

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 also is believed to be a function. Several plant lectins have been found to recognize noncarbohydrate ligands that are primarily hydrophobic in nature, including adenine, auxins, cytokinin, and indole acetic acid, as well as water-soluble porphyrins. These interactions may be physiologically relevant, since some of these molecules function as phytohormones. [10]

Lectin receptor kinases (LecRKs) are believed to recognize damage associated molecular patterns (DAMPs), which are created or released from herbivore attack.[ citation needed ] In Arabidopsis , legume-type LecRKs Clade 1 has 11 LecRK proteins. LecRK-1.8 has been reported to recognize extracellular NAD molecules and LecRK-1.9 has been reported to recognize extracellular ATP molecules.[ citation needed ]

Bacteria and viruses

Some hepatitis C viral glycoproteins may attach to C-type lectins on the host cell surface (liver cells) to initiate infection. [11] To avoid clearance from the body by the innate immune system, pathogens (e.g., virus particles and bacteria that infect human cells) often express surface lectins known as adhesins and hemagglutinins that bind to tissue-specific glycans on host cell-surface glycoproteins and glycolipids. [12] Multiple viruses, including influenza and several viruses in the Paramyxoviridae family, use this mechanism to bind and gain entry to target cells. [13]

Use

In medicine and medical research

Purified lectins are important in a clinical setting because they are used for blood typing. [14] Some of the glycolipids and glycoproteins on an individual's red blood cells can be identified by lectins.

In neuroscience, the anterograde labeling method is used to trace the path of efferent axons with PHA-L, a lectin from the kidney bean. [15]

A lectin (BanLec) from bananas inhibits HIV-1 in vitro. [16] Achylectins, isolated from Tachypleus tridentatus, show specific agglutinating activity against human A-type erythrocytes. Anti-B agglutinins such as anti-BCJ and anti-BLD separated from Charybdis japonica and Lymantria dispar, respectively, are of value both in routine blood grouping and research. [17]

In studying carbohydrate recognition by proteins

Lectin histochemistry of fish muscles infected by a myxozoan Parasite160010-fig2 - Lectins in Paralichthys olivaceus infected by Kudoa septempunctata - Lectin histochemistry.png
Lectin histochemistry of fish muscles infected by a myxozoan

Lectins from legume plants, such as PHA or concanavalin A, have been used widely 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.

Legume seed lectins have been studied for their insecticidal potential and have shown harmful effects for the development of pest. [18]

As a biochemical tool

Concanavalin A and other commercially available lectins have been used widely in affinity chromatography for purifying glycoproteins. [19]

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. [20]

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:

Dietary lectin

Leucoagglutinin is a toxic phytohemagglutinin found in raw Vicia faba (fava bean). Phytohemagglutinin L.png
Leucoagglutinin is a toxic phytohemagglutinin found in raw Vicia faba (fava bean).

Lectins are widespread in nature, and many foods contain the proteins. Some lectins can be harmful if poorly cooked or consumed in great quantities. They are most potent when raw as boiling, stewing or soaking in water for several hours can render most lectins inactive. Cooking raw beans at low heat, though, such as in a slow cooker, will not remove all the lectins. [21]

Some studies have found that lectins may interfere with absorption of some minerals, such as calcium, iron, phosphorus, and zinc. The binding of lectins to cells in the digestive tract may disrupt the breakdown and absorption of some nutrients, and as they bind to cells for long periods of time, some theories hold that they may play a role in certain inflammatory conditions such as rheumatoid arthritis and type 1 diabetes, but research supporting claims of long-term health effects in humans is limited and most existing studies have focused on developing countries where malnutrition may be a factor, or dietary choices are otherwise limited. [21]

Lectin-free diet

The first writer to advocate a lectin-free diet was Peter J. D'Adamo, a naturopathic physician best known for promoting the Blood type diet. He argued that lectins may damage a person's blood type by interfering with digestion, food metabolism, hormones, insulin production—and so should be avoided. [22] D'Adamo provided no scientific evidence nor published data for his claims, and his diet has been criticized for making inaccurate statements about biochemistry. [22] [23]

Steven Gundry proposed a lectin-free diet in his book The Plant Paradox (2017). It excludes a large range of commonplace foods including whole grains, legumes, and most fruit, as well as the nightshade vegetables: tomatoes, potatoes, eggplant, bell peppers, and chili peppers. [24] [25] Gundry's claims about lectins are considered pseudoscience. His book cites studies that have nothing to do with lectins, and some that show—contrary to his own recommendations—that avoiding the whole grains wheat, barley, and rye will allow increase of harmful bacteria while diminishing helpful bacteria. [26] [27] [28]

Toxicity

Lectins are one of many toxic constituents of many raw plants that are inactivated by proper processing and preparation (e.g., cooking with heat, fermentation). [29] For example, raw kidney beans naturally contain toxic levels of lectin (e.g. phytohaemagglutinin). Adverse effects may include nutritional deficiencies, and immune (allergic) reactions. [30]

Hemagglutination

Lectins are considered a major family of protein antinutrients, which are specific sugar-binding proteins exhibiting reversible carbohydrate-binding activities. [31] Lectins are similar to antibodies in their ability to agglutinate red blood cells. [32]

Many legume seeds have been proven to contain high lectin activity, termed hemagglutination. [33] Soybean is the most important grain legume crop in this category. Its seeds contain high activity of soybean lectins (soybean agglutinin or SBA).

History

Long before a deeper understanding of their numerous biological functions, the plant lectins, also known as phytohemagglutinins, were noted for their particularly high specificity for foreign glycoconjugates (e.g., those of fungi and animals) [34] and used in biomedicine for blood cell testing and in biochemistry for fractionation.[ citation needed ]

Although they were first discovered more than 100 years ago in plants, now lectins are known to be present throughout nature. The earliest description of a lectin is believed to have been 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. [35] The legume lectins are probably the most well-studied lectins.

See also

Related Research Articles

Glycomics is the comprehensive study of glycomes, including genetic, physiologic, pathologic, and other aspects. Glycomics "is the systematic study of all glycan structures of a given cell type or organism" and is a subset of glycobiology. The term glycomics is derived from the chemical prefix for sweetness or a sugar, "glyco-", and was formed to follow the omics naming convention established by genomics and proteomics.

<span class="mw-page-title-main">Glycoprotein</span> Protein with oligosaccharide modifications

Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.

An oligosaccharide is a saccharide polymer containing a small number of monosaccharides. Oligosaccharides can have many functions including cell recognition and cell adhesion.

<span class="mw-page-title-main">Glycolipid</span> Class of chemical compounds

Glycolipids are lipids with a carbohydrate attached by a glycosidic (covalent) bond. Their role is to maintain the stability of the cell membrane and to facilitate cellular recognition, which is crucial to the immune response and in the connections that allow cells to connect to one another to form tissues. Glycolipids are found on the surface of all eukaryotic cell membranes, where they extend from the phospholipid bilayer into the extracellular environment.

<span class="mw-page-title-main">Concanavalin A</span> Lectin (carbohydrate-binding protein) originally extracted from the jack-bean

Concanavalin A (ConA) is a lectin originally extracted from the jack-bean. It is a member of the legume lectin family. It binds specifically to certain structures found in various sugars, glycoproteins, and glycolipids, mainly internal and nonreducing terminal α-D-mannosyl and α-D-glucosyl groups. Its physiological function in plants, however, is still unknown. ConA is a plant mitogen, and is known for its ability to stimulate mouse T-cell subsets giving rise to four functionally distinct T cell populations, including precursors to regulatory T cells; a subset of human suppressor T-cells is also sensitive to ConA. ConA was the first lectin to be available on a commercial basis, and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities on the surface of various cells. It is also used to purify glycosylated macromolecules in lectin affinity chromatography, as well as to study immune regulation by various immune cells.

<span class="mw-page-title-main">DC-SIGN</span> Protein-coding gene in the species Homo sapiens

DC-SIGN also known as CD209 is a protein which in humans is encoded by the CD209 gene.

<span class="mw-page-title-main">Envelope glycoprotein GP120</span> Glycoprotein exposed on the surface of the HIV virus

Envelope glycoprotein GP120 is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Professors Tun-Hou Lee and Myron "Max" Essex of the Harvard School of Public Health in 1984. The 120 in its name comes from its molecular weight of 120 kDa. Gp120 is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate Proteoglycan and a specific interaction with the CD4 receptor, particularly on helper T-cells. Binding to CD4 induces the start of a cascade of conformational changes in gp120 and gp41 that lead to the fusion of the viral membrane with the host cell membrane. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

The terms glycans and polysaccharides are defined by IUPAC as synonyms meaning "compounds consisting of a large number of monosaccharides linked glycosidically". However, in practice the term glycan may also be used to refer to the carbohydrate portion of a glycoconjugate, such as a glycoprotein, glycolipid, or a proteoglycan, even if the carbohydrate is only an oligosaccharide. Glycans usually consist solely of O-glycosidic linkages of monosaccharides. For example, cellulose is a glycan composed of β-1,4-linked D-glucose, and chitin is a glycan composed of β-1,4-linked N-acetyl-D-glucosamine. Glycans can be homo- or heteropolymers of monosaccharide residues, and can be linear or branched.

Siglecs(Sialic acid-binding immunoglobulin-type lectins) are cell surface proteins that bind sialic acid. They are found primarily on the surface of immune cells and are a subset of the I-type lectins. There are 14 different mammalian Siglecs, providing an array of different functions based on cell surface receptor-ligand interactions.

<span class="mw-page-title-main">Galectin</span> Protein family binding to β-galactoside sugars

Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N-acetyllactosamine, which can be bound to proteins by either N-linked or O-linked glycosylation. They are also termed S-type lectins due to their dependency on disulphide bonds for stability and carbohydrate binding. There have been about 15 galectins discovered in mammals, encoded by the LGALS genes, which are numbered in a consecutive manner. Only galectin-1, -2, -3, -4, -7, -7B, -8, -9, -9B, 9C, -10, -12, -13, -14, and -16 have been identified in humans. Galectin-5 and -6 are found in rodents, whereas galectin-11 and -15 are uniquely found in sheep and goats. Members of the galectin family have also been discovered in other mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Unlike the majority of lectins they are not membrane bound, but soluble proteins with both intra- and extracellular functions. They have distinct but overlapping distributions but found primarily in the cytosol, nucleus, extracellular matrix or in circulation. Although many galectins must be secreted, they do not have a typical signal peptide required for classical secretion. The mechanism and reason for this non-classical secretion pathway is unknown.

<span class="mw-page-title-main">Langerin</span>

Langerin (CD207) is a type II transmembrane protein which is encoded by the CD207 gene in humans. It was discovered by scientists Sem Saeland and Jenny Valladeau as a main part of Birbeck granules. Langerin is C-type lectin receptor on Langerhans cells (LCs) and in mice also on dermal interstitial CD103+ dendritic cells (DC) and on resident CD8+ DC in lymph nodes.

The mannose receptor is a C-type lectin primarily present on the surface of macrophages, immature dendritic cells and liver sinusoidal endothelial cells, but is also expressed on the surface of skin cells such as human dermal fibroblasts and keratinocytes. It is the first member of a family of endocytic receptors that includes Endo180 (CD280), M-type PLA2R, and DEC-205 (CD205).

<span class="mw-page-title-main">CLEC4M</span> Protein-coding gene in the species Homo sapiens

C-type lectin domain family 4 member M is a protein that in humans is encoded by the CLEC4M gene. CLEC4M has also been designated as CD299.

<span class="mw-page-title-main">Viral neuraminidase</span>

Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Viral neuraminidase was discovered by Alfred Gottschalk at the Walter and Eliza Hall Institute in 1957. Neuraminidase inhibitors are antiviral agents that inhibit influenza viral neuraminidase activity and are of major importance in the control of influenza.

<span class="mw-page-title-main">Hemagglutinin</span>

In molecular biology, hemagglutinins are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae and Orthomyxoviridae families. Hemagglutinins are responsible for binding to receptors on red blood cells to initiate viral attachment and infection. The agglutination of red cells occurs when antibodies on one cell bind to those on others, causing amorphous aggregates of clumped cells.

Feline coronavirus (FCoV) is a positive-stranded RNA virus that infects cats worldwide. It is a coronavirus of the species Alphacoronavirus 1, which includes canine coronavirus (CCoV) and porcine transmissible gastroenteritis coronavirus (TGEV). FCoV has two different forms: feline enteric coronavirus (FECV), which infects the intestines, and feline infectious peritonitis virus (FIPV), which causes the disease feline infectious peritonitis (FIP).

BanLec is a lectin from the jacalin-related lectin family isolated from the fruit of the bananas Musa acuminata and Musa balbisiana. BanLec is one of the predominant proteins in the pulp of ripe bananas and has binding specificity for mannose and mannose-containing oligosaccharides. A 2010 study reported that BanLec was a potent inhibitor of HIV replication.

<span class="mw-page-title-main">Cell–cell recognition</span>

Cell–cell recognition is a cell's ability to distinguish one type of neighboring cell from another. This phenomenon occurs when complementary molecules on opposing cell surfaces meet. A receptor on one cell surface binds to its specific ligand on a nearby cell, initiating a cascade of events which regulate cell behaviors ranging from simple adhesion to complex cellular differentiation. Like other cellular functions, cell-cell recognition is impacted by detrimental mutations in the genes and proteins involved and is subject to error. The biological events that unfold due to cell-cell recognition are important for animal development, microbiomes, and human medicine.

Glycan arrays, like that offered by the Consortium for Functional Glycomics (CFG), National Center for Functional Glycomics (NCFG) and Z Biotech, LLC, contain carbohydrate compounds that can be screened with lectins, antibodies or cell receptors to define carbohydrate specificity and identify ligands. Glycan array screening works in much the same way as other microarray that is used for instance to study gene expression DNA microarrays or protein interaction Protein microarrays.

<span class="mw-page-title-main">Glycan-protein interactions</span> Class of biological intermolecular interactions

Glycan-Protein interactions represent a class of biomolecular interactions that occur between free or protein-bound glycans and their cognate binding partners. Intramolecular glycan-protein (protein-glycan) interactions occur between glycans and proteins that they are covalently attached to. Together with protein-protein interactions, they form a mechanistic basis for many essential cell processes, especially for cell-cell interactions and host-cell interactions. For instance, SARS-CoV-2, the causative agent of COVID-19, employs its extensively glycosylated spike (S) protein to bind to the ACE2 receptor, allowing it to enter host cells. The spike protein is a trimeric structure, with each subunit containing 22 N-glycosylation sites, making it an attractive target for vaccine search.

References

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  2. ↑ Brudner, Matthew; Karpel, Marshall; Lear, Calli; Chen, Li; Yantosca, L. Michael; Scully, Corinne; Sarraju, Ashish; Sokolovska, Anna; Zariffard, M. Reza; Eisen, Damon P.; et al. (April 2, 2013). Schneider, Bradley S. (ed.). "Lectin-Dependent Enhancement of Ebola Virus Infection via Soluble and Transmembrane C-type Lectin Receptors". PLOS ONE. 8 (4): e60838. Bibcode:2013PLoSO...860838B. doi: 10.1371/journal.pone.0060838 . PMC   3614905 . PMID   23573288.
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  21. 1 2 "Lectins". Harvard School of Public Health. 2019-01-24.
  22. 1 2 Goldstein, Myrna Chandler. (2002). Controversies in Food and Nutrition. Greenwood Press. pp. 221–222. ISBN   0-313-31787-9
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