Open AccessCharacterization and purification of porcine small intestinal mucus receptor for Escherichia coli K88ac fimbrial adhesin
Author(s) -
Jin L.Z,
Marquardt Ronald R,
Baidoo Samuel K,
Frohlich Andrew A
Publication year - 2000
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2000.tb01406.x
Subject(s) - bacterial adhesin , mucus , escherichia coli , mucin , pronase , biology , gel electrophoresis , biochemistry , fimbria , glycoprotein , receptor , enterotoxigenic escherichia coli , microbiology and biotechnology , sodium , sodium dodecyl sulfate , trypsin , chemistry , enzyme , enterotoxin , ecology , gene , organic chemistry
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 3 H‐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.