Nonfimbrial blood group N-specific adhesin (NFA-3) from Escherichia coli O20: KX104: H-, causing systemic infection

J. Grünberg, R. Perry, H. Hoschützky, B. Jann, K. Jann, J. Goldhar*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

From unfimbriated Escherichia coli O20 :KX104: H-, which caused systemic infection in man, and adhesin (NFA-3) was isolated by extraction from the bacteria in phosphate buffered saline at 70°C. It was purified by ammonium sulfate precipitation and anion exchange chromatography in the presence of urea. The adhesin had an apparent molecular weight in excess to 106 daltons and consisted of 17.500-d peptide subunits. It had an isoelectric point of 3.9 and contained one cysteine and no methionine. In haemagglutination assays and adhesion immunoassays, NFA-3 showed a preferred specificity for blood group N.

Original languageEnglish
Pages (from-to)241-245
Number of pages5
JournalFEMS Microbiology Letters
Volume56
Issue number2
DOIs
StatePublished - 1 Dec 1988

Keywords

  • Blood group N-specific adhesin
  • Escherichia coli haemagglutinin
  • Nonfimbrial adhesin

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