Abstract
Differentiation of Crohns disease-associated isolates from other pathogenic Escherichia coli by fimbrial adhesion under shear force
Highlights
The Gram-negative Escherichia coli (E. coli) species express type-1 pili or fimbriae, which are organelles integral to host receptor recognition and attachment [1]
We have shown that the adhesion of uropathogenic E. coli UTI89 can be conveniently studied by following the surface plasmon resonance (SPR) signals on the graphene-coated plasmonic interfaces [23,24]
Shear force enhancement has not been further investigated using E. coli isolates displaying a natural variation in FimH amino acids, which potentially plays a role in the allosteric regulation of receptor affinity for different E. coli pathotypes, until very recently [15]
Summary
The Gram-negative Escherichia coli (E. coli) species express type-1 pili or fimbriae, which are organelles integral to host receptor recognition and attachment [1]. With an N-terminal mannose-binding lectin domain connected by a flexible linker to a pilin anchoring it to FimG and FimF in the tip fibrillum. Natural variations in amino acid composition were found to regulate the pathoadaptivity of E. coli [3], not frequently in or near the conserved mannose-binding pocket, but predominantly at the interface between the lectin and pilin domains of the FimH TDA. The structural basis for these observations remained obscure, until the crystal structure of the whole tip of E. coli type-1 fimbriae Electron microscopic analysis already pointed to the importance of the incorporation of FimH into E. coli type-1 fimbriae to the extensibility of the stubby and flexible tip fibrillum [2].
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