Protein—sugar interactions A nuclear magnetic resonance investigation of the binding of <i>O</i>‐methyl‐di‐<i>N</i>‐acetyl‐β‐chitobioside to wheat germ agglutinin (lectin)

Grivet, Jean‐Philippe; Delmotte, Francis; Monsigny, Michel

doi:10.1016/0014-5793(78)80168-9

Cited by 18 publications

(3 citation statements)

References 30 publications

(29 reference statements)

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“…We may therefore postulate that the ring oxygen, the acetamido group on Cz and the hydroxyl group on C3 of N-acetylglucosamine (the ring oxygen, the acetamido group on Cs and the hydroxyl on C4 of N-acetylneuraminate) are involved in the binding to wheat-germ agglutinin. These conclusions are also supported by the nuclear magnetic resonance data [23] that directly show that the acetamido group of N-acetylglucosamine is involved in the binding, and by the lack of inhibition by 3-0-methyl-N-acetylglucosamine (Table 1) in agreement with [4]. The lack of inhibitory effect of N-glycoloylneuraminate could be related to the hydrophilic property and/or to the size of the glycoloyl group.…”

Section: Discussionsupporting

confidence: 79%

Sugar‐Lectin Interactions: How Does Wheat‐Germ Agglutinin Bind Sialoglycoconjugates?

Monsigny

Roche

Sène

et al. 1980

European Journal of Biochemistry

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428

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The specific binding of N-acetylneuraminic acid to wheat-germ agglutinin is based on configurational similarities between N-acetylneuraminic acid and N-acetylglucosamine. The N-acetamido group and an adjacent hydroxyl group, both in an equatorial position are shown to be the main determinants. The N-acetylneuraminic acid -wheat-germ agglutinin interaction is increased by the removal of the last two carbons Cs and C9. The interaction between wheat-germ agglutinin and glycoconjugates containing N-acetylneuraminic acid is shown to be dependent on a charge effect and on an avidity effect. Succinylated wheat-germ agglutinin which is negatively charged at physiological pH, in contrast with wheat-germ agglutinin which is positively charged, does not bind cell surface glycoconjugates containing N-acetylneuraminic acid but does bind cell surface glycoconjugates containing N-acetylglucosamine. The use of wheat-germ agglutinin and of SUCcinylated wheat-germ agglutinin leads to the determination of the number of cell surface receptors containing N-acetylneuramipic acid Wheat-germ agglutinin is a plant lectin which agglutinates various types of animal cells, of malignant cells and of protease-treated cells [l-31. The agglutination of cells is inhibited by N-acetylglucosamine and its /3l-4 oligomers [2,4]. In addition, wheat-germ agglutinin has been claimed to bind N-acetylneuraminic acid on the basis of equilibrium dialysis [5] and nuclear magnetic resonance [6] studies. Furthermore, the agglutination of neuraminidasetreated cells usually requires a higher concentration of wheat-germ agglutinin than required for untreated cells [2,7] although in some instances the neuraminidase treatment does not lower the cell agglutinability by the lectin [8]. Immobilized wheat germ agglutinin binds membrane sialoglycoproteins [9,10] but fails to bind the related sialoglycopeptides [9]. In the present paper, we wish to report several data showing that N-acetylneuraminic acid, gangliosides and glycoAbbreviations. Glc, glucose; Gal, galactose, NeuAc, N-acetylneuraminic acid ; NeuGc, N-glycoloylneuraminic acid ; Cer, ceramide; GM3, NeuAca2+3Gal~l+4GlcCer; GMz, GalNAc(3tZa-NeuAc)~l+4Gal~1+4GlcCer; GMI, Ga1/31+ 3GalNAc(3+2a-N e u A c )~l + 4 G a l~I -4GlcCer; GDI,, NeuAca2-3GalP1+3-GalNAc(3t2ctNeuAc)fll+4Gal~1-r4GlcCer; GDlb, Galpl -r 3-GalNAc(3+2aNeuAcXt2aNeuAc)~l+4Gal~I + 4GlcCer; GTl, NeuAcn2+ 3Gal/1'1+ 3GalNAc(3 + 2aNeuAcX t 2aNeuAc)flI -j 4-Gal81 +4GlcCer, Nph, p-nitrophenyl-.

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Section: Discussionsupporting

confidence: 79%

Sugar‐Lectin Interactions: How Does Wheat‐Germ Agglutinin Bind Sialoglycoconjugates?

Monsigny

Roche

Sène

et al. 1980

European Journal of Biochemistry

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428

201

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“…1968; Lanir & Navon, 1971) and to WGA in particular (Jordan et al, 1977(Jordan et al, , 1981Grivet et al, 1978;Lacelle, 1979). In the NMR experiments described below, intermediate exchange conditions prevailed at 24 ± 1 °C for all six titrations (K. A. Kronis and J. P. Carver, unpublished results).…”

mentioning

confidence: 99%

Specificity of isolectins of wheat germ agglutinin for sialyloligosaccharides: a 360-MHz proton NMR binding study

Ka¹,

Jp²

1982

Biochemistry

101

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The binding of three purified sialic acid containing oligosaccharides to two isolectins of wheat germ agglutinin (WGA I and WGA II) has been quantitated by measuring the broadening of a ligand resonance in the proton nuclear magnetic resonance (1H NMR) spectrum at 360 MHz. The ligands, isolated from bovine colostrum by using the procedure of Schneir and Rafelson [Schneir, M. L., & Rafelson, M. E., Jr. (1966) Biochim. Biophys, Acta 130, 1--11], were identified by 1H NMR as the alpha (2,3) and alpha (2,6) isomers of N-acetylneuraminyllactose, as well as the alpha (2,6) form of N,N'-diacetylneuraminyllactosamine. The dissociation constants, KD's, ranged from 0.7 to 10 mM (24 +/- 1 degree C). Two noteworthy features of WGA specificity emerge from an examination of the observed affinities: (1) both isolectins bind the alpha (2,3) isomer of N-acetylneuraminyllactose with higher affinity than the alpha (2,6) form and (2) WGA I binds two of the sialyloligosaccharides more tightly than does WGA II.

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“…The total line-shape analysis yielded z , z 0.2 s. This value is about an order of magnitude longer than the corresponding residence times found for the interaction of simple saccharides with other lectins such as wheat germ agglutinin [4], peanut agglutinin [6,7] and concanavalin A [3,1 I]. The relatively long T , for the binding of Galp(/31-4)GlcNAc to ECA indicates that the binding site of the lectin is highly complementary to that disaccharide unit, in analogy to the interaction of Galp(fl1-3)GalNAc with the extended binding site of peanut agglutinin ( T , z 4 s) [21,221.…”

mentioning

confidence: 70%

Binding of [1-13C]galactose-labeled N-acetyllactosamine to Erythrina cristagalli agglutinin as studied by 13C-NMR

et al. 1985

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The equilibrium binding kinetics of enzymatically prepared N‐acetyllactosamine to the lectin from Erythrina cristagalli have been investigated by 13C‐NMR spectroscopy. Under the experimental conditions used, NMR signals in the spectrum, corresponding to both the free and bound disaccharide species, were observed for the first time. This has permitted the simultaneous determinations of the equilibrium binding constant and the number of binding sites per lectin molecule. At the relatively high lectin concentrations used (0.3–0.87 mM), the association constants determined at 31°C (∼6×103 M−1) are typically lower then those obtained by other methods employing much lower lectin concentrations. Extrapolation of the experimentally observed values to infinite dilution gave a better fit of the data (Ka∼ 1.4×104 M−1) with the binding constant determined by other methods (K∼ 1.1×104 M−1). The sugar residence time on the lectin (∼0.2 s) was determined directly from the signal's line‐width using total line‐shape analysis. Similar NMR experiments may permit an analysis of the interaction of the lectin with glycoproteins and cells labelled with 13C‐enriched galactose residues. Moreover, information on lectin‐galactose interactions at the binding site may be obtained by using galactose labeled at various carbons.

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Protein—sugar interactions A nuclear magnetic resonance investigation of the binding of O‐methyl‐di‐N‐acetyl‐β‐chitobioside to wheat germ agglutinin (lectin)

Cited by 18 publications

References 30 publications

Sugar‐Lectin Interactions: How Does Wheat‐Germ Agglutinin Bind Sialoglycoconjugates?

Sugar‐Lectin Interactions: How Does Wheat‐Germ Agglutinin Bind Sialoglycoconjugates?

Specificity of isolectins of wheat germ agglutinin for sialyloligosaccharides: a 360-MHz proton NMR binding study

Binding of [1-13C]galactose-labeled N-acetyllactosamine to Erythrina cristagalli agglutinin as studied by 13C-NMR

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