Type 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coli.

ABSTRACT: Escherichia coli causes about 90% of urinary tract infections (UTI), and more than 95% of all UTI-causing E. coli express type 1 fimbriae. The fimbrial tip-positioned adhesive protein FimH utilizes a shear force-enhanced, so-called catch-bond mechanism of interaction with its receptor, mannose, where the lectin domain of FimH shifts from a low- to a high-affinity conformation upon separation from the anchoring pilin domain. Here, we show that immunization with the lectin domain induces antibodies that exclusively or predominantly recognize only the high-affinity conformation. In the lectin domain, we identified four high-affinity-specific epitopes, all positioned away from the mannose-binding pocket, which are recognized by 20 separate clones of monoclonal antibody. None of the monoclonal

SUBMITTER: Tchesnokova V 

PROVIDER: S-EPMC3187269 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature