Glycolipid modification of alpha 2 interferon binding. Sequence similarity between the alpha 2 interferon receptor and verotoxin (Shiga-like toxin) B-subunit

Biochem J. 1992 Apr 1;283 ( Pt 1)(Pt 1):25-6. doi: 10.1042/bj2830025.

Abstract

Previous studies have implicated the glycolipid receptor for the Escherichia coli-derived verotoxin, globotriaosylceramide (Gb3; Gal alpha 1-4Gal beta 1-4Glc-ceramide), in the mechanism of alpha 2 interferon signal transduction. Comparison of the amino acid sequence of the human alpha 2 interferon receptor with that of the B (receptor-binding)-subunit of verotoxin shows three regions of similarity which may provide a structural basis for alpha 2-interferon-receptor/Gb3 interaction.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins / genetics*
  • Bacterial Toxins / metabolism
  • Carbohydrate Sequence
  • Glycolipids / genetics*
  • Glycolipids / metabolism*
  • Humans
  • Macromolecular Substances
  • Molecular Sequence Data
  • Receptors, Cell Surface / genetics*
  • Receptors, Cell Surface / metabolism
  • Receptors, Immunologic / genetics*
  • Receptors, Immunologic / metabolism
  • Receptors, Interferon
  • Sequence Homology, Nucleic Acid
  • Shiga Toxin 1
  • Trihexosylceramides / metabolism

Substances

  • Bacterial Toxins
  • Glycolipids
  • Macromolecular Substances
  • Receptors, Cell Surface
  • Receptors, Immunologic
  • Receptors, Interferon
  • Shiga Toxin 1
  • Shiga-like toxin receptor
  • Trihexosylceramides
  • globotriaosylceramide