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 ]

Extraction of proteins and lectins can be extracted via similar processes, also with their analysis, and discovery. For example cottonseed contains compounds of interest within the studies of extraction and purification of proteins [11]

Bacteria and viruses

Some hepatitis C viral glycoproteins may attach to C-type lectins on the host cell surface (liver cells) to initiate infection. [12] 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. [13] Multiple viruses, including influenza and several viruses in the Paramyxoviridae family, use this mechanism to bind and gain entry to target cells. [14]

Use

In medicine and medical research

Purified lectins are important in a clinical setting because they are used for blood typing. [15] Some of the glycolipids and glycoproteins on an individual's red blood cells can be identified by lectins.

Non blood-group antigens 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. [16]

A lectin (BanLec) from bananas inhibits HIV-1 in vitro. [17] 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. [18]

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. [19]

As a biochemical tool

Concanavalin A and other commercially available lectins have been used widely in affinity chromatography for purifying glycoproteins. [20]

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. [21]

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. [22]

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. [22]

Lectin-free diet

The first writer to advocate a lectin-free diet was Peter J. D'Adamo, a Naturopath 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. [23] D'Adamo provided no scientific evidence nor published data for his claims, and his diet has been criticized for making inaccurate statements about biochemistry. [23] [24]

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. [25] [26] 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. [27] [28] [29]

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). [30] For example, raw kidney beans naturally contain toxic levels of lectin (e.g. phytohaemagglutinin). Adverse effects may include nutritional deficiencies, and immune (allergic) reactions. [31]

Hemagglutination

Lectins are considered a major family of protein antinutrients, which are specific sugar-binding proteins exhibiting reversible carbohydrate-binding activities. [32] Lectins are similar to antibodies in their ability to agglutinate red blood cells. [33]

Many legume seeds have been proven to contain high lectin activity, termed hemagglutination. [34] 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) [35] 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. [36] The legume lectins are probably the most well-studied lectins.

See also

Related Research Articles

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

Glycoproteins are proteins which contain oligosaccharide (sugar) 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.

Humoral immunity is the aspect of immunity that is mediated by macromolecules – including secreted antibodies, complement proteins, and certain antimicrobial peptides – located in extracellular fluids. Humoral immunity is named so because it involves substances found in the humors, or body fluids. It contrasts with cell-mediated immunity. Humoral immunity is also referred to as antibody-mediated immunity.

<span class="mw-page-title-main">Oligosaccharide</span> Saccharide polymer

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

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<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.

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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.

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<span class="mw-page-title-main">CLEC10A</span> Protein-coding gene in the species Homo sapiens

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References

  1. ↑ URS Rutishauser; Leo Sachs (May 1, 1975). "Cell-to-Cell Binding Induced by Different Lectins". Journal of Cell Biology. 65 (2): 247–257. doi:10.1083/jcb.65.2.247. PMC   2109424 . PMID   805150.
  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.
  3. ↑ Chan, Charles KF; Ransom, Ryan C; Longaker, Michael T (13 December 2016). "Lectins bring benefits to bones". eLife. 5. doi: 10.7554/eLife.22926 . PMC   5154756 . PMID   27960074.
  4. ↑ "Lectin list" (PDF). Interchim. 2010. Retrieved 2010-05-05.
  5. ↑ Boyd, W.C.; Shapleigh, E. (1954). "Specific precipitation activity of plant agglutinins (lectins)". Science. 119 (3091): 419. Bibcode:1954Sci...119..419B. doi:10.1126/science.119.3091.419. PMID   17842730.
  6. ↑ Walker, R. (2007). "The use of lectins in histopathology". Histopathology. 9 (10): 1121–1124. doi:10.1111/j.1365-2559.1985.tb02790.x. PMID   4085980. S2CID   24989148.
  7. ↑ Maverakis E, Kim K, Shimoda M, Gershwin M, Patel F, Wilken R, Raychaudhuri S, Ruhaak LR, Lebrilla CB (2015). "Glycans in the immune system and The Altered Glycan Theory of Autoimmunity". J Autoimmun. 57 (6): 1–13. doi:10.1016/j.jaut.2014.12.002. PMC   4340844 . PMID   25578468.
  8. ↑ Arasu, Abirami; Kumaresan, Venkatesh; Sathyamoorthi, Akila; Palanisamy, Rajesh; Prabha, Nagaram; Bhatt, Prasanth; Roy, Arpita; Thirumalai, Muthukumaresan Kuppusamy; Gnanam, Annie J.; Pasupuleti, Mukesh; Marimuthu, Kasi; Arockiaraj, Jesu (2013). "Fish lily type lectin-1 contains β-prism architecture: Immunological characterization". Molecular Immunology. 56 (4): 497–506. doi:10.1016/j.molimm.2013.06.020. PMID   23911406.
  9. ↑ Oldroyd, Giles E.D.; Downie, J. Allan (2008). "Coordinating Nodule Morphogenesis with Rhizobial Infection in Legumes". Annual Review of Plant Biology. 59: 519–546. doi:10.1146/annurev.arplant.59.032607.092839. PMID   18444906.
  10. ↑ Komath SS, Kavitha M, Swamy MJ (March 2006). "Beyond carbohydrate binding: new directions in plant lectin research". Org. Biomol. Chem. 4 (6): 973–988. doi:10.1039/b515446d. PMID   16525538.
  11. ↑ L.Y. Yatsu, T.J. Jacks, Association of lysosomal activity with aleurone grains in plant seeds, Archives of Biochemistry and Biophysics, Volume 124, 1968, Pages 466-471, ISSN 0003-9861, https://doi.org/10.1016/0003-9861(68)90354-8.
  12. ↑ R. Bartenschlager; S. Sparacio (2007). "Hepatitis C Virus Molecular Clones and Their Replication Capacity in Vivo and in Cell Culture". Virus Research. 127 (2): 195–207. doi:10.1016/j.virusres.2007.02.022. PMID   17428568.
  13. ↑ Soto, GE; Hultgren, SJ (1999). "Bacterial adhesins: common themes and variations in architecture and assembly". J Bacteriol. 181 (4): 1059–1071. doi:10.1128/JB.181.4.1059-1071.1999. PMC   93481 . PMID   9973330.
  14. ↑ Takimoto, Toru; Taylor, Garry L.; Connaris, Helen C.; Crennell, Susan J.; Portner, Allen (2002). "Role of the Hemagglutinin-Neuraminidase Protein in the Mechanism of Paramyxovirus-Cell Membrane Fusion". Journal of Virology. 76 (24): 13028–13033. doi:10.1128/JVI.76.24.13028-13033.2002. ISSN   0022-538X. PMC   136693 . PMID   12438628.
  15. ↑ Sharon, N.; Lis, H (2004). "History of lectins: From hemagglutinins to biological recognition molecules". Glycobiology. 14 (11): 53R–62R. doi: 10.1093/glycob/cwh122 . PMID   15229195.
  16. ↑ Carlson, Neil R. (2007). Physiology of behavior. Boston: Pearson Allyn & Bacon. ISBN   978-0-205-46724-2.
  17. ↑ Swanson, M. D.; Winter, H. C.; Goldstein, I. J.; Markovitz, D. M. (2010). "A Lectin Isolated from Bananas is a Potent Inhibitor of HIV Replication". Journal of Biological Chemistry. 285 (12): 8646–8655. doi: 10.1074/jbc.M109.034926 . PMC   2838287 . PMID   20080975.
  18. ↑ Viswambari Devi, R.; Basilrose, M. R.; Mercy, P. D. (2010). "Prospect for lectins in arthropods". Italian Journal of Zoology. 77 (3): 254–260. doi: 10.1080/11250003.2010.492794 . S2CID   84825587.
  19. ↑ Villegas-Coronado, Diana; Guzman-Partida, Ana María; Aispuro-Hernandez, Emmanuel; Vazquez-Moreno, Luz; Huerta-Ocampo, José Ángel; Sarabia-Sainz, José Andre-i; Teran-Saavedra, Nayelli Guadalupe; Minjarez-Osorio, Christian; Castro-Longoria, Reina; Maldonado, Amir; Lagarda-Diaz, Irlanda (2022). "Characterization and expression of prohibitin during the mexican bean weevil (Zabrotes subfasciatus, Boheman, 1833) larvae development". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 262: 110770. doi:10.1016/j.cbpb.2022.110770. PMID   35644320. S2CID   249145357.
  20. ↑ "Immobilized Lectin". legacy.gelifesciences.com.[ permanent dead link ]
  21. ↑ Glyco Station, Lec Chip, Glycan profiling technology Archived 2010-02-23 at the Wayback Machine
  22. 1 2 "Lectins". Harvard School of Public Health. 2019-01-24.
  23. 1 2 Goldstein, Myrna Chandler. (2002). Controversies in Food and Nutrition. Greenwood Press. pp. 221–222. ISBN   0-313-31787-9
  24. ↑ Stare, Fredrick John; Whelan, Elizabeth M. (1998). Fad-Free Nutrition. Hunter House Inc. pp. 209–212. ISBN   0-89793-237-4
  25. ↑ Rosenbloom, Cara. (2017). "Going 'lectin-free' is the latest pseudoscience diet fad". The Washington Post. Retrieved 25 August 2021.
  26. ↑ Amidor, Toby. (2017). "Ask the Expert: Clearing Up Lectin Misconceptions". Today's Dietitian. Vol. 19, No. 10, p. 10. Retrieved December 2021.
  27. ↑ Rosenbloom, Cara (7 July 2017). "Going 'lectin-free' is the latest pseudoscience diet fad". Washington Post . Retrieved 28 July 2017.
  28. ↑ Warner, Anthony (27 July 2017). "Lectin-free is the new food fad that deserves to be skewered". New Scientist . Retrieved 28 July 2017.
  29. ↑ T. Colin Campbell; Thomas Campbell (23 August 2017). 'The Plant Paradox' by Steven Gundry MD – A Commentary. Harper. ISBN   9780062427137.
  30. ↑ Taylor, Steve (2008). "40: Food Toxicology (Lectins: Cell-Agglutinating and Sugar-Specific Proteins)". In Metcalfe, Dean; Sampson, Hugh; Simon, Ronald (eds.). Food Allergy: Adverse Reactions to Foods and Food Additives (4th ed.). pp. 498–507.
  31. ↑ Cordain, Loren; Toohey, L.; Smith, M. J.; Hickey, M. S. (2007). "Modulation of immune function by dietary lectins in rheumatoid arthritis". British Journal of Nutrition. 83 (3): 207–217. doi: 10.1017/S0007114500000271 . PMID   10884708.
  32. ↑ Goldstein, Erwin; Hayes, Colleen (1978). The Lectins: Carbohydrate-Binding Proteins of Plants and Animals. Advances in Carbohydrate Chemistry and Biochemistry. Vol. 35. pp. 127–340. doi:10.1016/S0065-2318(08)60220-6. ISBN   978-0-12-007235-4. PMID   356549.
  33. ↑ Sharon, Nathan; Lis, Halina (1972). "Lectins: Cell-Agglutinating and Sugar-Specific Proteins". Science. 177 (4053): 949–959. Bibcode:1972Sci...177..949S. doi:10.1126/science.177.4053.949. PMID   5055944.
  34. ↑ Ellen, R.P.; Fillery, E.D.; Chan, K.H.; Grove, D.A. (1980). "Sialidase-Enhanced Lectin-Like Mechanism for Actinomyces viscosus and Actinomyces naeslundii Hemagglutination". Infection and Immunity. 27 (2): 335–343. doi: 10.1128/IAI.27.2.335-343.1980 . PMC   550769 . PMID   6769798.
  35. ↑ Els. J. M. Van Damme; Willy J. Peumans; llArpad Pusztai; Susan Bardocz (March 30, 1998). Handbook of Plant Lectins: Properties and Biomedical Applications. John Wiley & Sons. pp. 7–8. ISBN   978-0-471-96445-2 . Retrieved 18 April 2013.
  36. ↑ Aksakal, R.; Mertens, C.; Soete, M.; Badi, N.; Du Prez, F. (2021). "Applications of Discrete Synthetic Macromolecules in Life and Materials Science: Recent and Future Trends". Advanced Science. 2021 (2004038): 1–22. doi: 10.1002/advs.202004038 . PMC   7967060 . PMID   33747749.

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