2020年7月10日 · As the antibiotic therapeutic strategy has become less effective in the treatment of uropathogen-related UTIs, the anti-adhesive molecules active against fimbrial adhesins, key determinants of urovirulence, are attractive alternatives. The best-characterized bacterial adhesin is FimH, produced by uropathogenic Escherichia coli (UPEC).

FimH ligand binding affinity of A. early synthetic mannosides B. oligomannose-9 and subunits and C. other sugars. Herein, we comprehensively review rational ligand design and drug discovery strategies which have been employed to generate high-affinity, monovalent inhibitors of FimH.

2018年2月2日 · To gain a detailed insight into the binding kinetics of the interaction of FimH with mannoside ligands, surface plasmon resonance (SPR) measurements were performed (Table 4). The carboxyl-functionalized mannoside 5 (see supporting information for structure and synthesis) was immobilized via an ethylenediamine linker on a CM4 chip.

2010年5月14日 · The Escherichia coli fimbrial adhesive protein, FimH, mediates shear-dependent binding to mannosylated surfaces via force-enhanced allosteric catch bonds, but the underlying structural mechanism was previously unknown.

2013年10月25日 · Differential binding of FimH proteins from host-restricted and broad-host-range Salmonella to intestinal receptors was confirmed using mutant FimH adhesins obtained by site-directed mutagenesis. It was found that the low-binding variant of FimH from S .

2023年5月1日 · The binding affinities of dimannoses toward the FimH lectin have been determined using SPR, Molecular Mechanics Poisson-Boltzmann Surface Area (MM-PBSA) calculations, and a lectin profile kit, respectively.

2007年8月10日 · FimH is a mannose-specific adhesin located on the tip of type 1 fimbriae of Escherichia coli that is capable of mediating shear-enhanced bacterial adhesion. FimH consists of a fimbria-associated pilin domain and a mannose-binding lectin domain, with the binding pocket positioned opposite the interdomain interface.

SPR experiments with natural variants of FimH (e.g., aa. 158; Table 1) found in different E. coli strains corroborate the importance of the linker loop in the shear-dependent conformational change [22,46,47].

The FimH type-1 fimbrial adhesin allows pathogenic Escherichia coli to adhere to glycoproteins in the epithelial linings of human bladder and intestinal tract, by using multiple fimbriae...

Direct kinetic analysis using surface plasmon resonance (SPR) and glycoproteins carrying high-mannose carbohydrate chains (RNase B, horseradish peroxidase and mannan-BSA) revealed the existence of high- and low-adhesive allelic variants, not only in S. Typhimurium but also in …