Digalactosylceramide is the receptor for staphylococcal enterotoxin-B in human kidney proximal tubular cells

Subroto B Chatterjee, Madhu Khullar, Wan Y. Shi

Research output: Contribution to journalArticle

Abstract

We have characterized a glycosphingolipid (GSL) receptor for Staphylococcus enterotoxin-B (SEB) in cultured human kidney proximal tubular (PT) cells. Solid-phase binding of [125I]SEB to the GSL receptor was concentration dependent and was not displaceable by two structurally related toxins, such as staphylococcal enterotoxin-A and toxic shock syndrome toxin-1. Rat kidney cells did not bind [125I]SEB. However, when the rat kidney cells were pre-incubated with digalactosylceramide, there was a concentration-dependent binding of [125I]SEB. Trimethylsilyl derivatization of methyl glycosides, followed by gas-liquid chromatography-mass spectrometry (GC-MS), revealed that galactose was the major sugar component of this putative receptor GSL. The sphingosines present in this GSL were d18:2, d22:2 and d23:0; the fatty acids present were palmitate, oleate and stearate. Permethvlation of alditol acetates and GC-MS revealed two predominant sugars, namely 2, 3, 4 and 6 tetramethylgalactital and 2, 3 and 6 trimethylgalactital. The GSL receptor for SEB was sensitive to a-galactosidase, and resistant to (3-galactosidase and fi-glucosidase. Taken together, our studies reveal that the tentative structure of the receptor for SEB in human kidney PT cells is CerGalα1→4Gal. In summary, we have identified a GSL as one of the binding sites of SEB, a food-borne toxin. We believe that our finding may open up rational approaches for the therapy of SEB-induced glycopathology in man.

Original languageEnglish (US)
Pages (from-to)327-333
Number of pages7
JournalGlycobiology
Volume5
Issue number3
DOIs
StatePublished - May 1995

Fingerprint

Liquid chromatography
Kidney
Sugars
Gas chromatography
Glycosphingolipids
Receptor
Mass spectrometry
Rats
Sphingosines
Glycosides
Cell
Binding sites
Fatty acids
Mass Spectrometry
Chromatography
Galactosidases
Liquid
Gas Chromatography-Mass Spectrometry
Dependent
Fatty Acids

Keywords

  • GC-MS
  • Glycosphingolipids
  • Proximal tubular cells
  • Staphylococcal enterotoxin-B

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Public Health, Environmental and Occupational Health
  • Neuropsychology and Physiological Psychology
  • Hematology
  • Biochemistry

Cite this

Digalactosylceramide is the receptor for staphylococcal enterotoxin-B in human kidney proximal tubular cells. / Chatterjee, Subroto B; Khullar, Madhu; Shi, Wan Y.

In: Glycobiology, Vol. 5, No. 3, 05.1995, p. 327-333.

Research output: Contribution to journalArticle

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AB - We have characterized a glycosphingolipid (GSL) receptor for Staphylococcus enterotoxin-B (SEB) in cultured human kidney proximal tubular (PT) cells. Solid-phase binding of [125I]SEB to the GSL receptor was concentration dependent and was not displaceable by two structurally related toxins, such as staphylococcal enterotoxin-A and toxic shock syndrome toxin-1. Rat kidney cells did not bind [125I]SEB. However, when the rat kidney cells were pre-incubated with digalactosylceramide, there was a concentration-dependent binding of [125I]SEB. Trimethylsilyl derivatization of methyl glycosides, followed by gas-liquid chromatography-mass spectrometry (GC-MS), revealed that galactose was the major sugar component of this putative receptor GSL. The sphingosines present in this GSL were d18:2, d22:2 and d23:0; the fatty acids present were palmitate, oleate and stearate. Permethvlation of alditol acetates and GC-MS revealed two predominant sugars, namely 2, 3, 4 and 6 tetramethylgalactital and 2, 3 and 6 trimethylgalactital. The GSL receptor for SEB was sensitive to a-galactosidase, and resistant to (3-galactosidase and fi-glucosidase. Taken together, our studies reveal that the tentative structure of the receptor for SEB in human kidney PT cells is CerGalα1→4Gal. In summary, we have identified a GSL as one of the binding sites of SEB, a food-borne toxin. We believe that our finding may open up rational approaches for the therapy of SEB-induced glycopathology in man.

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