Structural and functional study of the receptor binding site for FimH adhesin in uropathogenic strains of Escherichia coli

We evaluated binding capacity of FimH-FocH hybrid adhesins during their interaction with model 1M and 3M substrates and epithelial cells. Introduction of the Glu89Lys point mutation into the filmH gene induced a new 1M-specific phenotype of adhesin. The role of a new pathoadaptive sign in the population of E. coli is discussed.

Authors
Trinchina E.V.
Publisher
New York Consultants BureauSpringer / Автономная некоммерческая организация Издательство Российской академии медицинских наук
Number of issue
4
Language
English
Pages
380-384
Status
Published
Volume
136
Year
2003
Keywords
Escherichia coli; type 1 pili; FimH-FocH hybrid adhesin; 1M-specific phenotype
Date of creation
19.10.2018
Date of change
19.10.2018
Short link
https://repository.rudn.ru/en/records/article/record/8926/
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