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

The objectives of this study were to investigate the nature of, and to puri fy K88ac fimbrial adhesin-specific receptors in the mucus from the small in testine of piglet. Adhesion was studied by incubating H-3-labeled Escherich ia coli with mucus that were treated with or without pronase, proteinase, t rypsin or sodium metaperiodate. The results indicated that treatment with e ither proteolytic enzymes or sodium metaperiodate (to oxidize sugars) signi ficantly 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 l east in part, glycoprotein in nature. The K88+MB fimbriae specific receptor was purified using affinity chromatography. Sodium dodecyl sulfate-polyacr ylamide gel electrophoresis of the purified K88+MB specific receptor togeth er with the above data suggested that the receptor from the mucus of the sm all intestine of the pig was a 80-kDa glycoprotein. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.