Glycoconjugate Journal

, Volume 33, Issue 5, pp 819–836 | Cite as

Novel interactions of complex carbohydrates with peanut (PNA), Ricinus communis (RCA-I), Sambucus nigra (SNA-I) and wheat germ (WGA) agglutinins as revealed by the binding specificities of these lectins towards mucin core-2 O-linked and N-linked glycans and related structures

  • E.V. ChandrasekaranEmail author
  • Jun Xue
  • Jie Xia
  • Siraj D. Khaja
  • Conrad F. Piskorz
  • Robert D. Locke
  • Sriram Neelamegham
  • Khushi L. MattaEmail author
Original Article


Plant lectins through their multivalent quaternary structures bind intrinsically flexible oligosaccharides. They recognize fine structural differences in carbohydrates and interact with different sequences in mucin core 2 or complex-type N-glycan chain and also in healthy and malignant tissues. They are used in characterizing cellular and extracellular glycoconjugates modified in pathological processes. We study here, the complex carbohydrate-lectin interactions by determining the effects of substituents in mucin core 2 tetrasaccharide Galβ1-4GlcNAcβ1-6(Galβ1-3)GalNAcα-O-R and fetuin glycopeptides on their binding to agarose-immobilized lectins PNA, RCA-I, SNA-I and WGA. Briefly, in mucin core 2 tetrasaccharide (i) structures modified by α2-3/6-Sialyl LacNAc, LewisX and α1-3-Galactosyl LacNAc resulted in regular binding to PNA whereas compounds with 6-sulfo LacNAc displayed no-binding; (ii) strucures bearing α2-6-sialyl 6-sulfo LacNAc, or 6-sialyl LacdiNAc carbohydrates displayed strong binding to SNA-I; (iii) structures with α2-3/6-sialyl, α1-3Gal LacNAc or LewisX were non-binder to RCA-I and compounds with 6-sulfo LacNAc only displayed weak binding; (iv) structures containing LewisX, 6-Sulfo LewisX, α2-3/6-sialyl LacNAc, α2-3/6-sialyl 6-sulfo LacNAc and GalNAc Lewis-a were non-binding to WGA, those with α1-2Fucosyl, α1-3-Galactosyl LacNAc, α2-3-sialyl T-hapten plus 3ʹ/6ʹsulfo LacNAc displayed weak binding, and compounds with α2-3-sialyl T-hapten, α2.6-Sialyl LacdiNAc, α2-3-sialyl D-Fucβ1-3 GalNAc and Fucα-1-2 D-Fucβ-1-3GalNAc displaying regular binding and GalNAc LewisX and LacdiNAc plus D-Fuc β-1-3 GalNAcα resulting in tight binding. RCA-I binds Fetuin triantennary asialoglycopeptide 100 % after α-2-3 and 25 % after α-2-6 sialylation, 30 % after α-1-2 and 100 % after α-1-3 fucosylation, and 50 % after α-1-3 galactosylation. WGA binds 3-but not 6-Fucosyl chitobiose core. Thus, information on the influence of complex carbohydrate chain constituents on lectin binding is apparently essential for the potential application of lectins in glycoconjugate research.


Plant lectins Binding specificities Complex glycans Mucin core-2 compounds N-linked glycans Carbohydrate chain constituents 



Acrylyamide copolymer


Aleuria aurantia lectin






Blood group antigen


Bovine serum albumin


Bovine submaxillary mucin


Cowper’s gland mucin


Cytidine 5′ monophosphate


Fetuin O-glycosidic


Fetuin triantennary




Galβ1, 4GlcNAc



Mucin Core 2



Pig gastric mucin


Peanut agglutinin


Ricinus communis agglutinin-I


Sambucus nigra agglutinin-I








Wheat germ agglutinin



The study was supported by NIH Grants CA 35329; HL103411 and DOD grant W81XWH-06-1-0013.


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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  • E.V. Chandrasekaran
    • 1
    Email author
  • Jun Xue
    • 1
  • Jie Xia
    • 1
  • Siraj D. Khaja
    • 1
  • Conrad F. Piskorz
    • 1
  • Robert D. Locke
    • 1
  • Sriram Neelamegham
    • 2
  • Khushi L. Matta
    • 1
    • 2
    Email author
  1. 1.Department of Cancer BiologyRoswell Park Cancer InstituteBuffaloUSA
  2. 2.Department of Chemical and Biological EngineeringState University of New YorkBuffaloUSA

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