fimH Antibody

1. Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain. PMID: 29180452
2. Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. PMID: 28246638
3. A mutant missing the type 1 pilus-associated adhesin FimH displayed somewhat reduced persistence within the gut. PMID: 29311232
4. The authors demonstrated that FimH residues E50 and T53 are crucial for adhesion under flow conditions. PMID: 27816993
5. In the absence of tensile force, the FimH pilin domain allosterically accelerates spontaneous ligand dissociation from the FimH lectin domain by 100,000-fold. PMID: 26948702
6. mouse urothelium responds to the adhesion of type 1-fimbriated UPEC by activating dual ligand/receptor system, one between FimH adhesin and uroplakin Ia and another between lipopolysaccharide and Tlr4. PMID: 26549759
7. Luteolin decreased the attachment and invasion of UPEC in bladder epithelial cells down-regulating the expression of adhesin fimH gene PMID: 25051393
8. Data indicate that thiazolylaminomannosides prevented bacterial attachment to the gut by blocking the FimH bacterial adhesin. PMID: 23795713
9. New promising vaccine combinations based on the FliC antigen against urinary tract infections caused by uropathogenic Escherichia coli. PMID: 23220068
10. analyzed mutational patterns in the fimH gene of mucosa-associated E. coli strains isolated from IBD and non-IBD pediatric patients to investigate microevolution of this genetic trait; study found some FimH variants that seem to be more involved than others in evolution of inflammatory bowel disease pathogenesis PMID: 22290143
11. FimH elicits an immune response that enhances cell adhesion of Escherichia coli. PMID: 21768279
12. Study presents the crystal structure of FimH incorporated into the multiprotein fimbrial tip, where the anchoring (pilin) domain of FimH interacts with the mannose-binding (lectin) domain and causes a twist in the beta sandwich fold of the latter. PMID: 20478255
13. Co-immunoprecipitation experiments in the presence of alpha-methyl mannose verified the binding of Escherichia coli FimH to ATP synthase beta-subunit of human brain microvascular endothelial cells. PMID: 20067530
14. the single A62S mutation altered phase variation, reducing the proportion of piliated cells, reduced mannose binding 8-fold, and decreased bladder colonization 30-fold in vivo compared to wild-type PMID: 20018753
15. FimH adhesin activated the murine microglial cell line, BV-2, which resulted in the production of nitric oxide and the release of tumor necrosis factor-alpha. PMID: 16036224
16. analysis of trimannose versus monomannose interactions with the FimH adhesin of Escherichia coli PMID: 16624825
17. Stability of the FimH-mannose bond. PMID: 16933977
18. findings indicate that FimH induces host cell signalling cascades that are involved in E. coli K1 invasion of human brain microvascular endothelial cells (HBMEC) and CD48 is a putative HBMEC receptor for FimH PMID: 17222190
19. Functional trade-offs may determine the natural populational instability of this mutation or other pathoadaptive FimH mutations that confer dramatic increases in 1M binding strength. PMID: 17502398
20. analysis of how interdomain interactions in the FimH adhesin of Escherichia coli regulate the affinity to mannose PMID: 17567583
21. Data show that removal of the cysteine bond in the mannose-binding domain of FimH did not affect FimH-mannose binding under static or low shear conditions, but the adhesion level was substantially decreased under increased fluid flow. PMID: 17697252
22. integrin-like allosteric link between the binding pocket and the interdomain conformation can serve as the basis for the catch bond property of FimH and, possibly, other adhesive proteins. PMID: 18174167
23. Deletion of fimH resulted in lost of agglutination ability. PMID: 18438011
24. Naturally occurring mutations in the signal peptides of the adhesive, tip-associated subunit of type 1 fimbriae (FimH) are positively selected in uropathogenic Escherichia coli. PMID: 18664574
25. The authors show by cryo-electron microscopy that FimH binding to the extracellular domain of UP Ia induces global conformational changes in the entire UP receptor complex, including a coordinated movement of the tightly bundled transmembrane helices. PMID: 19577575

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KEGG: ecj:JW4283

STRING: 316407.85677063