Characterization and purification of porcine small intestinal mucus receptor for Escherichia coli K88ac fimbrial adhesin

L. Z. Jin, Ronald R. Marquardt, Samuel K Baidoo, Andrew A. Frohlich

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


The objectives of this study were to investigate the nature of, and to purify K88ac fimbrial adhesin-specific receptors in the mucus from the small intestine of piglet. Adhesion was studied by incubating 3H-labeled Escherichia coli with mucus that were treated with or without pronase, proteinase, trypsin or sodium metaperiodate. The results indicated that treatment with either proteolytic enzymes or sodium metaperiodate (to oxidize sugars) significantly reduced E. coli K88ac or K88+MB adhesion to the mucus, suggesting that the K88ac and K88+MB specific receptors in this preparation were, at least in part, glycoprotein in nature. The K88+MB fimbriae specific receptor was purified using affinity chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified K88+MB specific receptor together with the above data suggested that the receptor from the mucus of the small intestine of the pig was a 80-kDa glycoprotein. Copyright (C) 2000 Federation of European Microbiological Societies.

Original languageEnglish (US)
Pages (from-to)17-22
Number of pages6
JournalFEMS Immunology and Medical Microbiology
Issue number1
StatePublished - Jan 2000

Bibliographical note

Funding Information:
This research was financially supported by The National Science and Engineering Council of Canada (NSERC), Agri-Food Research and Development Initiatives (ARDI) and the Industrial Research Assistance Program (IRAP).


  • Affinity chromatography
  • Escherichia coli K88
  • Intestinal mucus receptor
  • Swine

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