Binding of Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to G(M1), derivatives of G(M1), and nonlipid oligosaccharide polyvalent ligands

Cara-Lynne Schengrund, N. J. Ringler

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Abstract

Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli have been shown to differ somewhat in their ligand specificity and in the antigenicity of their binding sites. Therefore, the components of the oligosaccharide portion of G(M1) bound by cholera toxin and the heat-labile enterotoxin of E. coli were identified by determining the concentration of G(M1), derivatives of G(M1), oligosaccharide isolated from G(M1), or clustered oligosaccharide needed to inhibit toxin binding to G(M1)-coated plastic wells. The K(I)S for G(M1), the C(7) sialosyl aldehyde of G(M1), and ethanolamine-sialosyl-G(M1) were similar (~ 30-50 nM) for both toxins. N-Deacetylation of G(M1) resulted in a small increase in K(I); formation of the sialosyl methyl ester increased the K(I) 2-5 fold; loss of the terminal galactosyl residue (G(M2)) increased the K(I) by 10-15-fold; and removal of the sialosyl moiety (asialo-G(M1)) resulted in loss of inhibition of both toxins. Oligosaccharide isolated from G(M1) had a K(I) for both toxins that was ~ 100-fold greater than that obtained for G(M1) and ~ 1000-fold greater than that for a clustered oligosaccharide derivative having an average of 8 oligosaccharide residues (isolated from G(M1)) per molecule of poly-L-lysine. These results indicate that both toxins are functionally quite similar in their recognition of G(M1) as a ligand in that each requires the free carboxyl group of sialic acid for optimum binding, does not need carbons 8 and 9 of the sialosyl moiety nor the acetyl groups associated with the sialic acid and galactosamine residues, and can have its binding to G(M1) blocked by a nonlipid compound, i.e. oligo-G(M1)-poly-L-lysine.

Original languageEnglish (US)
Pages (from-to)13233-13237
Number of pages5
JournalJournal of Biological Chemistry
Volume264
Issue number22
StatePublished - Jan 1 1989

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Vibrio cholerae
Enterotoxins
Cholera Toxin
Oligosaccharides
Escherichia coli
Hot Temperature
N-Acetylneuraminic Acid
Ligands
Derivatives
Lysine
Galactosamine
Ethanolamine
Aldehydes
Plastics
Esters
Carbon
Binding Sites
Molecules
G(M1)-oligosaccharide

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{5b0a15112e3a4762ab54b64d20563e6e,
title = "Binding of Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to G(M1), derivatives of G(M1), and nonlipid oligosaccharide polyvalent ligands",
abstract = "Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli have been shown to differ somewhat in their ligand specificity and in the antigenicity of their binding sites. Therefore, the components of the oligosaccharide portion of G(M1) bound by cholera toxin and the heat-labile enterotoxin of E. coli were identified by determining the concentration of G(M1), derivatives of G(M1), oligosaccharide isolated from G(M1), or clustered oligosaccharide needed to inhibit toxin binding to G(M1)-coated plastic wells. The K(I)S for G(M1), the C(7) sialosyl aldehyde of G(M1), and ethanolamine-sialosyl-G(M1) were similar (~ 30-50 nM) for both toxins. N-Deacetylation of G(M1) resulted in a small increase in K(I); formation of the sialosyl methyl ester increased the K(I) 2-5 fold; loss of the terminal galactosyl residue (G(M2)) increased the K(I) by 10-15-fold; and removal of the sialosyl moiety (asialo-G(M1)) resulted in loss of inhibition of both toxins. Oligosaccharide isolated from G(M1) had a K(I) for both toxins that was ~ 100-fold greater than that obtained for G(M1) and ~ 1000-fold greater than that for a clustered oligosaccharide derivative having an average of 8 oligosaccharide residues (isolated from G(M1)) per molecule of poly-L-lysine. These results indicate that both toxins are functionally quite similar in their recognition of G(M1) as a ligand in that each requires the free carboxyl group of sialic acid for optimum binding, does not need carbons 8 and 9 of the sialosyl moiety nor the acetyl groups associated with the sialic acid and galactosamine residues, and can have its binding to G(M1) blocked by a nonlipid compound, i.e. oligo-G(M1)-poly-L-lysine.",
author = "Cara-Lynne Schengrund and Ringler, {N. J.}",
year = "1989",
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Binding of Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to G(M1), derivatives of G(M1), and nonlipid oligosaccharide polyvalent ligands. / Schengrund, Cara-Lynne; Ringler, N. J.

In: Journal of Biological Chemistry, Vol. 264, No. 22, 01.01.1989, p. 13233-13237.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Binding of Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to G(M1), derivatives of G(M1), and nonlipid oligosaccharide polyvalent ligands

AU - Schengrund, Cara-Lynne

AU - Ringler, N. J.

PY - 1989/1/1

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N2 - Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli have been shown to differ somewhat in their ligand specificity and in the antigenicity of their binding sites. Therefore, the components of the oligosaccharide portion of G(M1) bound by cholera toxin and the heat-labile enterotoxin of E. coli were identified by determining the concentration of G(M1), derivatives of G(M1), oligosaccharide isolated from G(M1), or clustered oligosaccharide needed to inhibit toxin binding to G(M1)-coated plastic wells. The K(I)S for G(M1), the C(7) sialosyl aldehyde of G(M1), and ethanolamine-sialosyl-G(M1) were similar (~ 30-50 nM) for both toxins. N-Deacetylation of G(M1) resulted in a small increase in K(I); formation of the sialosyl methyl ester increased the K(I) 2-5 fold; loss of the terminal galactosyl residue (G(M2)) increased the K(I) by 10-15-fold; and removal of the sialosyl moiety (asialo-G(M1)) resulted in loss of inhibition of both toxins. Oligosaccharide isolated from G(M1) had a K(I) for both toxins that was ~ 100-fold greater than that obtained for G(M1) and ~ 1000-fold greater than that for a clustered oligosaccharide derivative having an average of 8 oligosaccharide residues (isolated from G(M1)) per molecule of poly-L-lysine. These results indicate that both toxins are functionally quite similar in their recognition of G(M1) as a ligand in that each requires the free carboxyl group of sialic acid for optimum binding, does not need carbons 8 and 9 of the sialosyl moiety nor the acetyl groups associated with the sialic acid and galactosamine residues, and can have its binding to G(M1) blocked by a nonlipid compound, i.e. oligo-G(M1)-poly-L-lysine.

AB - Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli have been shown to differ somewhat in their ligand specificity and in the antigenicity of their binding sites. Therefore, the components of the oligosaccharide portion of G(M1) bound by cholera toxin and the heat-labile enterotoxin of E. coli were identified by determining the concentration of G(M1), derivatives of G(M1), oligosaccharide isolated from G(M1), or clustered oligosaccharide needed to inhibit toxin binding to G(M1)-coated plastic wells. The K(I)S for G(M1), the C(7) sialosyl aldehyde of G(M1), and ethanolamine-sialosyl-G(M1) were similar (~ 30-50 nM) for both toxins. N-Deacetylation of G(M1) resulted in a small increase in K(I); formation of the sialosyl methyl ester increased the K(I) 2-5 fold; loss of the terminal galactosyl residue (G(M2)) increased the K(I) by 10-15-fold; and removal of the sialosyl moiety (asialo-G(M1)) resulted in loss of inhibition of both toxins. Oligosaccharide isolated from G(M1) had a K(I) for both toxins that was ~ 100-fold greater than that obtained for G(M1) and ~ 1000-fold greater than that for a clustered oligosaccharide derivative having an average of 8 oligosaccharide residues (isolated from G(M1)) per molecule of poly-L-lysine. These results indicate that both toxins are functionally quite similar in their recognition of G(M1) as a ligand in that each requires the free carboxyl group of sialic acid for optimum binding, does not need carbons 8 and 9 of the sialosyl moiety nor the acetyl groups associated with the sialic acid and galactosamine residues, and can have its binding to G(M1) blocked by a nonlipid compound, i.e. oligo-G(M1)-poly-L-lysine.

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