On-cell saturation transfer difference NMR for the identification of FimH ligands and inhibitors

Volume: 112, Pages: 104876 - 104876
Published: Jul 1, 2021
Abstract
We describe the development of an on-cell NMR method for the rapid screening of FimH ligands and the structural identification of ligand binding epitopes. FimH is a mannose-binding bacterial adhesin expressed at the apical end of type 1 pili of uropathogenic bacterial strains and responsible for their d-mannose sensitive adhesion to host mammalian epithelial cells. Because of these properties, FimH is a key virulence factor and an attractive...
Paper Details
Title
On-cell saturation transfer difference NMR for the identification of FimH ligands and inhibitors
Published Date
Jul 1, 2021
Volume
112
Pages
104876 - 104876
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