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Characterization of the adhesin of Escherichia coli F18 fimbriae.


ABSTRACT: Previous research has suggested that the adhesin encoded by the F18 fimbrial operon in Escherichia coli is either the FedE or FedF protein. In this work, we show that anti-FedF antibodies, unlike anti-FedE serum, were able to inhibit E. coli adhesion to porcine enterocytes. Moreover, specific adhesion to enterocytes was shown with purified FedF-maltose binding protein.

SUBMITTER: Smeds A 

PROVIDER: S-EPMC98896 | biostudies-literature | 2001 Dec

REPOSITORIES: biostudies-literature

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Characterization of the adhesin of Escherichia coli F18 fimbriae.

Smeds A A   Hemmann K K   Jakava-Viljanen M M   Pelkonen S S   Imberechts H H   Palva A A  

Infection and immunity 20011201 12


Previous research has suggested that the adhesin encoded by the F18 fimbrial operon in Escherichia coli is either the FedE or FedF protein. In this work, we show that anti-FedF antibodies, unlike anti-FedE serum, were able to inhibit E. coli adhesion to porcine enterocytes. Moreover, specific adhesion to enterocytes was shown with purified FedF-maltose binding protein. ...[more]

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