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PMID: 272642 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Diphtheria toxin has the properties of a lectin.

Draper RK, Chin D, Simon MI

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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26 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1978-01-00
Pages
261-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC411226
Subset
IM
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