PapG adhesin from E. coli J96 recognizes the same saccharide epitope when present on whole bacteria and as isolated protein

Ulf Nilsson, Robert T. Striker, Scott J. Hultgren, Göran Magnusson

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Purified PapG adhesin from the genetically well-defined uropathogenic Escherichia coli strain J96, as well as whole bacteria, were bound to microtiter plates that carried covalently bound globotetraose and galabiose. The binding was inhibited by soluble saccharide derivatives corresponding to the globoseries of glycolipids, including all di-, tri-, tetra-, and pentasaccharide fragments of the Forssman antigen and all monodeoxy analogues of galabiose. Analysis of the inhibition pattern showed no significant difference between purified adhesin and whole bacteria. The glucose unit at the reducing end of the natural saccharides was detrimental to PapG binding since deletion of the glucose unit increased the inhibitory power 10-20 fold. The five hydroxyl groups HO-6, -2', -3', -4', -6' of the galabiose unit were shown to be important for PapG binding, presumably via intermolecular hydrogen bonds.

Original languageEnglish
Pages (from-to)1809-1817
Number of pages9
JournalBioorganic and Medicinal Chemistry
Volume4
Issue number11
DOIs
StatePublished - Nov 1 1996

Keywords

  • E. coli J96
  • Forssman-related saccharides
  • Galabiose binding epitope
  • Microtiter plate ELISA
  • PapG adhesin

Fingerprint Dive into the research topics of 'PapG adhesin from E. coli J96 recognizes the same saccharide epitope when present on whole bacteria and as isolated protein'. Together they form a unique fingerprint.

Cite this