Journal article
Expression and purification of the mannose recognition domain of the FimH adhesin
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.
| Language: | English |
|---|---|
| Year: | 2000 |
| Pages: | 147-151 |
| ISSN: | 15746968 and 03781097 |
| Types: | Journal article |
| DOI: | 10.1111/j.1574-6968.2000.tb09186.x |
Adhesins, Bacterial Adhesins, Escherichia coli Artificial Gene Fusion Bacterial Vaccines Blotting, Western Chromatography, Affinity DNA Primers Escherichia coli Escherichia coli Vaccines FimH Fimbriae Proteins Gene Expression Genetic Vectors Lectins, C-Type Mannose Receptor Mannose-Binding Lectins Mannose-binding domain Receptors, Cell Surface Type 1 fimbria fimH protein, E coli
