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Salmonella choleraesuis and Escherichia coli K88 show lectin like activity to IgA Oligosaccharides
Author(s) -
RamosClamont Gabriela,
Guzman Roberto,
Winzerling Joy,
VazquezMoreno Luz
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a57-a
Subject(s) - bacterial adhesin , enterotoxigenic escherichia coli , microbiology and biotechnology , salmonella , lectin , fimbria , escherichia coli , antibody , mucin , immunoglobulin a , biotinylation , biology , affinity chromatography , enterobacteriaceae , isotype , salmonella enteritidis , bacteria , immunoglobulin g , biochemistry , monoclonal antibody , immunology , enterotoxin , genetics , gene , enzyme
Salmonella choleraesuis and enteric Escherichia coli K88 have been recognized as etiologic agents of diarrhea in neonatal and weaned pigs. Adhesion of bacteria to receptors on intestinal epithelialcells, mediated by lectin‐ like fimbriae, is the initial step for infection. Serum preparations containing high concentration of immunoglobulins (Igs) improve piglet survival during diarrhea, presumably by interfering with adhesin interaction with gut tissues, however reliable commercial sources of porcine Igs are limited. We isolated Igs from pig serum and tested their activity in limiting adhesin interactions to piglet small intestine. Serum IgG, IgA and IgM were isolated in a single step using highly acetylated agarose (HA) hydrophobic interaction chromatography. Further purification of each Igs was done by affinity chromatography. K88 lectin biotinylated via its amino groups exhibited a characteristic binding to IgA oligosaccharides but not to those from IgG or IgM. IgA binding inhibited the adherence of K88 strains to porcine intestinal mucins. On the contrary, Salmonella choleraesuis did not interacted with IgA oligosaccharides.