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.
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 3'/6'sulfo 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.
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA. gchandrasek@yahoo.com.
E V
EV
Chandrasekaran
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA.
Jun
J
Xue
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA.
Jie
J
Xia
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA.
Siraj D
SD
Khaja
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA.
Conrad F
CF
Piskorz
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA.
Robert D
RD
Locke
Department of Chemical and Biological Engineering, State University of New York, Buffalo, NY, 14260, USA.
Sriram
S
Neelamegham
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY, 14263, USA. klmatta40@gmail.com.|Department of Chemical and Biological Engineering, State University of New York, Buffalo, NY, 14260, USA. klmatta40@gmail.com.
Khushi L
KL
Matta
D010367:Arachis / Q000737:chemistry*; D006020:Glycopeptides / Q000737:chemistry*; D037121:Plant Lectins / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry*; D012278:Ricinus / Q000737:chemistry*; D027924:Sambucus nigra / Q000737:chemistry*; D014908:Triticum / Q000737:chemistry*
D006020:Glycopeptides; D037121:Plant Lectins; D011134:Polysaccharides
Binding specificities; Carbohydrate chain constituents; Complex glycans; Mucin core-2 compounds; N-linked glycans; Plant lectins