Open AccessExpression and purification of the mannose recognition domain of the FimH adhesin
Author(s) -
Schembri Mark A,
Hasman Henrik,
Klemm Per
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09186.x
Subject(s) - bacterial adhesin , mannose , microbiology and biotechnology , domain (mathematical analysis) , chemistry , biology , biochemistry , escherichia coli , gene , mathematics , mathematical analysis
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 α‐ 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.