Production of fimbrial adhesins K99 and F41 by enterotoxigenic Escherichia coli as a function of growth-rate domain
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چکیده
منابع مشابه
Characterization of the F41 fimbrial antigen of enterotoxigenic Escherichia coli by using monoclonal antibodies.
We produced monoclonal antibodies (MAbs) from 23 different murine hybridoma cell lines against the F41 fimbrial antigen of bovine and porcine enterotoxigenic Escherichia coli. Cell lines were created by fusing myeloma cells and spleen cells of mice that were immunized with either purified F41 or with Formalin-killed whole cells. The specificity of the MAbs to the F41 antigen was proven by enzym...
متن کاملIsolation and structural characterization of the equine erythrocyte receptor for enterotoxigenic Escherichia coli K99 fimbrial adhesin.
The erythrocyte receptor for Escherichia coli K99 fimbrial adhesin was isolated from equine erythrocytes and characterized as Neu5Gc-alpha(2----3)-Galp-beta(1----4)-GLcp-beta(1----1)-Ceramide. This glycolipid acted as the receptor for K99 by four different experimental approaches: inhibition of equine erythrocyte hemagglutination by preincubation of K99-positive bacteria or purified K99 fimbria...
متن کاملStructural Sampling of Glycan Interaction Profiles Reveals Mucosal Receptors for Fimbrial Adhesins of Enterotoxigenic Escherichia coli
Fimbriae are long, proteinaceous adhesion organelles expressed on the bacterial envelope, evolutionarily adapted by Escherichia coli strains for the colonization of epithelial linings. Using glycan arrays of the Consortium for Functional Glycomics (CFG), the lectin domains were screened of the fimbrial adhesins F17G and FedF from enterotoxigenic E. coli (ETEC) and of the FimH adhesin from uropa...
متن کاملAnalysis of a naturally occurring K99+ enterotoxigenic Escherichia coli strain that fails to produce K99.
A spontaneously occurring field isolate of enterotoxigenic Escherichia coli that was genotypically K99+ but phenotypically K99- was analyzed for the reason that it did not express K99. The defect, which was cis active, was located within an area 5' to the first gene required for K99 biogenesis and was the result of the deletion of a single base pair.
متن کاملHeterobinary adhesins based on the Escherichia coli FimH fimbrial protein.
The FimH adhesin of Escherichia coli type 1 fimbriae confers the ability to bind to D-mannosides by virtue of a receptor-binding domain located in its N-terminal region. This protein was engineered into a heterobifunctional adhesin by introducing a secondary binding site in the C-terminal region. The insertion of histidine clusters into this site resulted in coordination of various metal ions b...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1985
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.49.1.159-163.1985