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FEMS Microbiol Lett. 2000 Jul 15;188(2):147-51.

Expression and purification of the mannose recognition domain of the FimH adhesin.

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1
Department of Microbiology, Bldg 301, Technical University of Denmark, DK-2800, Lyngby, Denmark.

Abstract

Type 1 fimbriae have been shown to be specifically required for Escherichia coli colonisation and pathogenesis of the urinary tract. These structural organelles mediate specific adhesion to alpha-D-mannosides by virtue of the FimH adhesin. FimH is a two-domain protein in which the N-terminal domain contains the receptor-binding site and the C-terminal domain is required for organelle integration. To date, FimH has only been isolated as a complex with the system-specific chaperone FimC. Here we report that a functional form of the FimH receptor-binding domain can be readily isolated and characterised by replacing the C-terminal domain with a histidine tag.

PMID:
10913698
[Indexed for MEDLINE]
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