Abstract
The inhibition of protein synthesis in Chinese hamster V79 cells by diphtheria toxin is antagonized by the lectins concanavalin A, succinylated concanavalin A, and wheat germ agglutinin but not by Proteus vulgaris phytohemagglutinin or abrus agglutinin. The effects of concanavalin A and wheat germ agglutinin are reversed by methyl alpha-mannoside and N-acetylglucosamine, respectively. The inhibition of diphtheria toxin as a function of concanavalin A concentration fits a model of competitive inhibition with an apparent dissociation constant for concanavalin A of 3 X 10(-8) M. These results suggest that the diphtheria toxin receptor may be an oligosaccharide. To test this hypothesis, we screened several oligosaccharides for the ability to inhibit diphtheria toxin. The cell wall polysaccharide of Salmonella cholera suis and the ovalbumin glycopeptide were effective inhibitors. These studies suggest that diphtheria toxin may have the oligosaccharide binding properties of a lectin with specificity for N-acetylglucosamine and mannose.
MeSH Terms
Cell Line
Concanavalin A/pharmacology
Diphtheria Antitoxin
Lectins/pharmacology
Oligosaccharides/pharmacology
Plant Lectins
Polysaccharides, Bacterial/pharmacology
Protein Biosynthesis
Receptors, Drug/drug effects
Structure-Activity Relationship
Triticum
Chemicals
Diphtheria Antitoxin
Lectins
Oligosaccharides
Plant Lectins
Polysaccharides, Bacterial
Receptors, Drug
Concanavalin A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Draper R K
Chin D
Simon M I
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