Glycolipid receptor binding specificity of exoenzyme S from Pseudomonas aeruginosa

Biochem Biophys Res Commun. 1991 Mar 29;175(3):1076-81. doi: 10.1016/0006-291x(91)91675-3.

Abstract

By use of the tlc overlay procedure we have shown that exoenzyme S extracted from cultures of Pseudomonas aeruginosa specifically binds to the glycolipids asialoGM1, asialoGM2 and to a lesser extent lactosyl ceramide. More significantly, strong binding was also observed to the glycerolipid receptor we have detected for Helicobacter pylori (Lancet ii, 238-241.1989). Exoenzyme S can be extracted in a toxic and nontoxic form. Toxicity correlated with ability to bind the H. pylori receptor. This species was the only receptor detected in the most sensitive cell lines. The relative binding of exoenzyme S to the ganglio series glycolipids and the glycerolipid receptor was modified in a reciprocal manner in the presence of metal ions, suggesting that exoenzyme S has two interrelated receptor binding sites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP Ribose Transferases*
  • Bacteria / immunology
  • Bacterial Toxins*
  • Calcium Chloride / pharmacology
  • Cell Line
  • Chromatography, Thin Layer / methods
  • Edetic Acid / pharmacology
  • Gangliosides
  • Glycolipids / metabolism*
  • Glycosphingolipids / metabolism
  • Gram-Negative Anaerobic Bacteria / immunology
  • Humans
  • Magnesium Chloride / pharmacology
  • Poly(ADP-ribose) Polymerases / metabolism*
  • Protein Binding
  • Pseudomonas aeruginosa / enzymology*
  • Receptors, Cell Surface*
  • Receptors, Immunologic / metabolism*
  • Substrate Specificity

Substances

  • Bacterial Toxins
  • Gangliosides
  • Glycolipids
  • Glycosphingolipids
  • Receptors, Cell Surface
  • Receptors, Immunologic
  • glycolipid receptor
  • Magnesium Chloride
  • ganglio-N-triaosylceramide
  • Edetic Acid
  • ADP Ribose Transferases
  • Poly(ADP-ribose) Polymerases
  • exoenzyme S
  • Calcium Chloride