Skip to main content
SpringerLink
Log in

Plant Lectins

  • Chapter
  • First Online:
Lectins

  • 399 Accesses

Abstract

Lectins are a group of proteins with specific carbohydrate binding proteins that are found abundant in nature, especially within the kingdom Plantae. Several plant lectins are isolated and well characterised within the chemical, physico-chemical and biological properties. Plant lectins have the potential to agglutinate red blood cells with specific carbohydrate entities due to the existence of a minimum of one non-catalytic domain that binds reversibly to specific recognised monosaccharides or oligosaccharides without a change it’s moiety. In this chapter, we discuss plant lectins, a wide ranging and well characterised group which were discovered 100 years ago. It includes history, production, purification, classification, function and also the application of plant lectins. Most of the plant lectins show extensive biological responses like the need for anti-insect, anti-viral, anti-fungal and immunomodulatory functions in modern research. Plant lectins have proved their potential in crop improvement and also their wide use in biomedical research.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 189.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 249.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 249.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Abbreviations

AIDS:

Acquired Immunodeficiency Syndrome

BMGY:

Buffered complex glycerol medium

cDNA:

Complementary DNA

ConA:

Concanavalin A

E. coli :

Escherichia coli

GalNAc:

N-Acetylgalactosamine

GBL:

Galactose-binding lectin

GMP:

Good manufacturing practices

HeLa cells:

Henrietta Lacks cells

HIV:

Human Immunodeficiency Virus

HTLV:

Human T-lymphotropic Virus

LPS:

Lipopolysaccharides

MCF7:

Michigan Cancer Foundation-7

PEG:

Polyethylene glycol

RCA:

Ricinus communis agglutinin

RIP:

Ribosome inactivating proteins

SBA:

Soybean agglutinin

SBL:

Soybean lectin

UEA:

Ulex europaeus

WGA:

Wheat Germ Agglutinin

References

  • Allen AK (1996) Potato lectin: a three-domain glycoprotein with novel hydroxyproline containing sequences and sequence similarities to wheat-germ agglutinin. Int J Biochem Cell Biol 28(11):1285–1291

    CAS  PubMed  Google Scholar 

  • Barbieri L, Battelli MG, Stirpe F (1993) Ribosome-inactivating proteins from plants. Biochim Biophys Acta Rev Biomembr 1154(3–4):237–282

    CAS  Google Scholar 

  • Barkai-Golan R, Mirelman D, Sharon N (1978) Studies on growth inhibition by lectins of Penicillia and Aspergilli. Arch Microbial 116:119–124

    CAS  Google Scholar 

  • Beintema JJ, Peumans WJ (1992) The primary structure of stinging nettle (Urtica dioica) agglutinin A two-domain member of the hevein family. FEBS Lett 299(2):131–134

    CAS  PubMed  Google Scholar 

  • Cheung AH, Wong JH, Ng TB (2009) Musa acuminata (Del Monte banana) lectin is fructose-binding lectin with cytokine-inducing activity. Phytomedicine 16:594–600

    Google Scholar 

  • Choi SH, Lyu SY, Park WB (2004) Mistletoe lectin induces apoptosis and telomerase inhibition in human A253 cancer cells through dephosphorylation of Akt. Arch Pharm Res 27:68–76

    CAS  PubMed  Google Scholar 

  • Collinge DB (1993) Plant chitinases. Plant J 3(1):31–40

    CAS  PubMed  Google Scholar 

  • Does MP, Houterman PM, Dekker HL, Cornelissen BJ (1999) Processing, targeting, and antifungal activity of stinging nettle agglutinin in transgenic tobacco. Plant Physiol 120:421–432

    CAS  PubMed  PubMed Central  Google Scholar 

  • Doyle RI, Nedjat-Haiern F, Keller KF, Frasch CE (1984) J Clin Microbiol 19:383–387

    CAS  PubMed  PubMed Central  Google Scholar 

  • Edelman GM, Cunningham BA, Reeke GN Jr, Becker JW, Waxdal MJ, Wang JL (1972) The covalent and three-dimensional structure of concanavalin A. Proc Natl Acad Sci U S A 69:2580–2584

    CAS  PubMed  PubMed Central  Google Scholar 

  • El-Aassar M et al (2014) Microencapsulation of lectin anti-cancer agent and controlled release by alginate beads, biosafety approach. Int J Biol Macromol 69:88–94

    CAS  PubMed  Google Scholar 

  • Elfstrand M (1898) Über blutkörperchen agglutinierende Eiweisse. In: Kobert R (ed) Görbersdorfer veröffentlichungen a Band I. Enke, Stuttgart, pp 1–159

    Google Scholar 

  • Etzler ME (1985) Plant lectins: molecular and biological aspects. Annu Rev Plant Physiol Plant Mol Biol 36:209–234

    CAS  Google Scholar 

  • Etzler ME (1986) Distribution and function of plant lectins. In: Liener IE, Sharon N, Goldstein IJ (eds) The lectins: properties, functions, and applications in biology and medicine. Academic, Orlando, FL, pp 371–435

    Google Scholar 

  • Gershoni JM (1985) Trends Biochem Sci 10:103–106

    CAS  Google Scholar 

  • Goldstein IJ, Hughes RC, Monsigny M, Osawa T, Sharon N (1980) What should be called a lectin? Nature 285:66

    Google Scholar 

  • Gray A, Flatt P (1999) Insulin-secreting activity of the traditional antidiabetic plant Viscum album (mistletoe). J Endocrinol 160(3):409–414

    CAS  PubMed  Google Scholar 

  • Hamid R et al (2013) Lectins: proteins with diverse applications. J Appl Pharm Sci 3(4.1):93–103

    Google Scholar 

  • Hardman KD, Ainsworth CF (1972) Structure of concanavalin A at 2.4 Å resolution. Biochemistry 11(26):4910–4919. https://doi.org/10.1021/bi00776a006

    Article  CAS  PubMed  Google Scholar 

  • Hashim OH, Jayapalan JJ, Lee C-S (2017) Lectins: an effective tool for screening of potential cancer biomarkers. PeerJ 5:e3784

    PubMed  PubMed Central  Google Scholar 

  • Iordache F et al (2015) Antimicrobial and antiparasitic activity of lectins. Curr Pharmaceut Biotechnol 16(2):152–161

    CAS  Google Scholar 

  • Keyaerts E, Vijgen L, Pannecouque C, Van Damme E, Peumans W, Egberink H, Balzarini J, Van Ranst M (2007) Plant lectins are potent inhibitors of coronaviruses by interfering with two targets in the viral replication cycle. Antivir Res 75:179–187

    CAS  PubMed  Google Scholar 

  • Khan F, Khan MI (2011) Fungal lectins: current molecular and biochemical perspectives. Int J Biol Chem 5(1):20

    Google Scholar 

  • Koeppe SJ, Rupnow J (1988) Purification and characterization of a lectin from the seeds of amaranth (Amaranthus cruentus). J Food Sci 53(5):1412–1417

    CAS  Google Scholar 

  • Kolb H et al (1986) Suppression of low-dose streptozotocin-induced diabetes by immunomodulatory lectins. Diabetes Res 3(4):183–186

    CAS  PubMed  Google Scholar 

  • Lagarda-Diaz I, Guzman-Partida A, Vazquez-Moreno L (2017) Legume lectins: proteins with diverse applications. Int J Mol Sci 18(6):1242

    PubMed Central  Google Scholar 

  • Lam SK, Ng TB (2011) Lectins: production and practical applications. Appl Microbiol Biotechnol 89(1):45–55

    CAS  PubMed  Google Scholar 

  • Landsteiner K, Raubitschek H (1907) Observations on hemolysis and hemagglutination. C Bakt 45:660–665

    Google Scholar 

  • Lannoo N, Van Damme EJM (2014) Lectin domains at the frontiers of plant defense. Front Plant Sci 5:397

    PubMed  PubMed Central  Google Scholar 

  • Lannoo N, Vervecken W, Proost P, Rougé P, Van Damme EJ (2007) Expression of the nucleocytoplasmic tobacco lectin in the yeast Pichia pastoris. Protein Expr Purif 53:275–282

    CAS  PubMed  Google Scholar 

  • LeVine D, Kaplan MJ, Greenaway PJ (1972) The purification and characterization of wheatgerm agglutinin. Biochem J 129(4):847–856

    CAS  PubMed  PubMed Central  Google Scholar 

  • Li YR, Liu QH, Wang HX, Ng TB (2008) A novel lectin with potent antitumor, mitogenic and HIV-1 reverse transcriptase inhibitory activities from the edible mushroom Pleurotus citrinopileatus. Biochim Biophys Acta 1780:51–57

    CAS  PubMed  Google Scholar 

  • Liener I (2012) The lectins: properties, functions, and applications in biology and medicine. Elsevier

    Google Scholar 

  • Lin P, Ye X, Ng T (2008) Purification of melibiose-binding lectins from two cultivars of Chinese black soybeans. Acta Biochim Biophys Sin Shanghai 40:1029–1038

    CAS  PubMed  Google Scholar 

  • Liu J (1996) Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy. Biochemistry 35(5):1516–1524

    CAS  PubMed  Google Scholar 

  • Majumder P, Mondal HA, Das S (2005) Insecticidal activity of Arum maculatum tuber lectin and its binding to the glycosylated insect gut receptors. J Agric Food Chem 53:6725–6729

    CAS  PubMed  Google Scholar 

  • Mirelman D, Galun E, Sharon N, Lotan R (1975) Inhibition of fungal growth by wheat germ agglutinin. Nature 256:414–416

    CAS  PubMed  Google Scholar 

  • Mishkind M, Raikhe NV, Palevitz BA, Keegstra K (1982) J Cell Biol 92:753–764

    CAS  PubMed  Google Scholar 

  • Naeem A, Haque S, Khan RH (2007) Purification and characterization of a novel beta-d-galactosides-specific lectin from Clitoria ternatea. Protein J 26:403–413. https://doi.org/10.1007/s10930-007-9080-5

    Article  CAS  PubMed  Google Scholar 

  • Nagata Y, Burger MM (1972) Wheat germ agglutinin isolation and crystallization. JBiolChem 247(7):2248–2250

    CAS  Google Scholar 

  • Oliveira C, Felix W, Moreira RA, Teixeira JA, Domingues L (2008) Expression of frutalin, an alpha-D-galactose-binding jacalin related lectin, in the yeast Pichia pastoris. Protein Expr Purif 60:188–193

    CAS  PubMed  Google Scholar 

  • Oliveira C, Costa S, Teixeira JA, Domingues L (2009) cDNA cloning and functional expression of the alpha-D-galactose-binding lectin frutalin in Escherichia coli. Mol Biotechnol 43:212–220

    CAS  PubMed  Google Scholar 

  • Peumans WJ, Van Damme EJM (1995) Lectins as plant defense proteins. Plant Physiol 109:347–352

    CAS  PubMed  PubMed Central  Google Scholar 

  • Pihíková D, Kasák P, Tkac J (2015) Glycoprofiling of cancer biomarkers: label–free electrochemical lectin–based biosensors. Open Chem 13:636–655

    PubMed  PubMed Central  Google Scholar 

  • Pilobello KT, Mahal LK (2007) Lectin microarrays for glycoprotein analysis. Methods Mol Biol 385:193–203

    CAS  PubMed  Google Scholar 

  • Read SM, Northcote DH (1983) Subunit structure and interactions of the phloem proteins of Cucurbita maxima (pumpkin). Eur J Biochem 134(3):561–569

    CAS  PubMed  Google Scholar 

  • Rinderle SJ (1989) Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, that recognizes the T-(or cryptic T)-antigen. J Biol Chem 264(27):16123–16131

    CAS  PubMed  Google Scholar 

  • Schrevel J, Gros D, Monsigny M (1981) Prog Histochem Cytochem 4(2):1–269

    Google Scholar 

  • Sharon N, Lis H (1990) Legume lectins – a large family of homologous proteins. FASEB J 4:3198–3208

    CAS  PubMed  Google Scholar 

  • Sharon N, Lis H (2004) History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology 14(11):53R–62R

    CAS  PubMed  Google Scholar 

  • Sobral APV et al (2010) ConA and UEA-I lectin histochemistry of parotid gland mucoepidermoid carcinoma. J Oral Sci 52(1):49–54

    CAS  PubMed  Google Scholar 

  • Strosberg AD, Buffard D, Lauwereys M, Foriers A (1986) Legume lectins: a large family of homologous proteins. In: Liener IE, Sharon N, Goldstein IJ (eds) The lectins, properties, functions, and applications in biology and medicine. Academic, Orlando, FL, pp 249–264

    Google Scholar 

  • Sumner JB, Howell SF (1936) The identification of the hemagglutinin of the Jack bean with concanavalin A. J Bacteriol 32:227–237

    CAS  PubMed  PubMed Central  Google Scholar 

  • Tateno H, Winter HC, Goldstein IJ (2004) Cloning, expression in Escherichia coli and characterization of the recombinant Neu5-Acalpha2, 6Galbeta1, 4GlcNAc-specific high-affinity lectin and its mutants from the mushroom polyporus squamosus. Biochem J 382:667–675

    CAS  PubMed  PubMed Central  Google Scholar 

  • Transue TR (1997) Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin. Nat StructBiol 4(10):779–783

    CAS  Google Scholar 

  • Upadhyay SK, Saurabh S, Rai P, Singh R, Chandrashekar K, Verma PC, Singh PK, Tuli R (2010) SUMO fusion facilitates expression and purification of garlic leaf lectin but modifies some of its properties. J Biotechnol 146:1–8

    CAS  PubMed  Google Scholar 

  • Van Damme EJ (1999) Characterization and molecular cloning of the lectin from Helianthus tuberosus. Eur J Biochem 259(1–2):135–142

    PubMed  Google Scholar 

  • Van Damme EJ, Allen AK, Peumans WJ (1987) Isolation and characterization of a lectin with exclusive specificity towards mannose from snowdrop (Galanthus nivalis) bulbs. FEBS Lett 215(1):140–144

    Google Scholar 

  • Van Damme EJM, Smeets K, Peumans WJ (1995) The mannose-binding monocot lectins and their genes. In: Lectins: biomedical perspectives, pp 59–80

    Google Scholar 

  • Van Damme EJ, Barre A, Rougé P, Van Leuven F, Peumans WJ (1997) Isolation and molecular cloning of a novel type 2 ribosome-inactivating protein with an inactive B chain from elderberry (Sambucus nigra) bark. J Biol Chem 272(13):8353–8360

    PubMed  Google Scholar 

  • Van Damme EJM, Peumans WJ, Barre A, Rougé P (1998) Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit Rev Plant Sci 17:575–692

    Google Scholar 

  • Van Damme EJM, Lannoo N, Peumans WJ (2008) Plant lectins. Adv Bot Res 48:107–209

    Google Scholar 

  • Van Parijs J (1991) Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 183(2):258–264

    PubMed  Google Scholar 

  • Vodkin LO, Rhodes PR, Goldberg RB (1983) A lectin gene insertion has the structural features of a transposable element. Cell 34:1023–1031

    CAS  PubMed  Google Scholar 

  • Watkins WM, Morgan WTJ (1952) Neutralization of the anti-H agglutinin in eel by simple sugars. Nature 169:825–826

    CAS  PubMed  Google Scholar 

  • Wick MR, Hornick JL (2011) Immunohistology of soft tissue and osseous neoplasms in diagnostic immunohistochemistry, 3rd edn

    Google Scholar 

  • Wright CS (1990) 2· 2 Å resolution structure analysis of two refined N-acetylneuraminyl-lactose wheat germ agglutinin isolectin complexes. J Mol Biol 215(4):635–651

    CAS  PubMed  Google Scholar 

  • Zenteno E, Ochoa J-L (1988) Purification of a lectin from Amaranthus leucocarpus by affinity chromatography. Phytochemistry 27(2):313–317

    CAS  Google Scholar 

  • Zhang C, Medina-Bolivar F, Buswell S, Cramer CL (2005) Purification and stabilization of ricin B from tobacco hairy root culture medium by aqueous two-phase extraction. J Biotechnol 117:39–48

    CAS  PubMed  Google Scholar 

Download references

Acknowledgments

We are thankful for the kind support from Kerala University of fisheries and ocean studies, Kochi, India.

Author information

Authors and Affiliations

  1. Kerala University of Fisheries and Ocean Studies, Kochi, Kerala, India

    Abdullah Bin Abdul Nazar, Aneetta Skinner & Debarghya Ghosh Dastidar

  2. Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Cochin, Kerala, India

    Preetham Elumalai

Authors
  1. Abdullah Bin Abdul Nazar
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Aneetta Skinner
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Debarghya Ghosh Dastidar
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Preetham Elumalai
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Preetham Elumalai .

Editor information

Editors and Affiliations

  1. Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Cochin, Kerala, India

    Preetham Elumalai

  2. School of Ocean Science and Technology, Kerala University of Fisheries and Ocean Studies, Cochin, Kerala, India

    Sreeja Lakshmi

Ethics declarations

The authors have no conflicts of interest to declare.

Rights and permissions

Reprints and permissions

Copyright information

© 2021 The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.

About this chapter

Check for updates. Verify currency and authenticity via CrossMark

Cite this chapter

Nazar, A.B.A., Skinner, A., Dastidar, D.G., Elumalai, P. (2021). Plant Lectins. In: Elumalai, P., Lakshmi, S. (eds) Lectins. Springer, Singapore. https://doi.org/10.1007/978-981-16-7462-4_6

Download citation

Publish with us

Policies and ethics

Search

Navigation