Effect of heat-stable enterotoxin of Escherichia coli on cultured mammalian cells

D. D. Thomas, F. C. Knoop

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

The binding of biologically active 125I-labeled heat-stable enterotoxin (ST) of Escherichia coli with mammalian cells was dose dependent and could be inhibited with low concentrations of unlabeled toxin or by neutralization with specific antiserum. There was positive cooperativity among cell binding sites. A single cultured cell bound ~4 X 104 molecules of ST; the dissociation constant was 1.33 X 10-10 M. The specific binding of ST was partially inhibited by Pronase® (Sigma Chemical Company, St. Louis, Missouri) and trypsin, but not by lipid- or carbohydrate-specific emzymes, simple sugars, or saccharides. Addition of ST to cultures of rat basophilic leukemia cells resulted in a dose-dependent secretion of histamine. Pharmacologic agents that inhibited calcium uptake or prostaglandin synthesis decreased the amount of histamine released. These data demonstrate the specific binding of ST by cultured cells and support the contention that calcium and prostaglandins may be important in the molecular mechanism(s) whereby ST activates guanylate cyclase.

Original languageEnglish (US)
Pages (from-to)450-459
Number of pages10
JournalJournal of Infectious Diseases
Volume147
Issue number3
DOIs
StatePublished - Jan 1 1983

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Infectious Diseases

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