Expression and purification of the mannose recognition domain of the FimH adhesin |
| |
Authors: | Schembri M A Hasman H Klemm P |
| |
Institution: | 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. |
| |
Keywords: | FimH Mannose-binding domain Type 1 fimbria |
本文献已被 PubMed 等数据库收录! |
|