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. 2016 Nov 5;36(3):467–478. doi: 10.1007/s10096-016-2820-8

Table 1.

Overview of the mutations generated in MSC95-FimH and adhesion to 1 M and 3 M

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The ability of E. coli FimH mutants to adhere to mannose substrates under flow and to agglutinate yeast. Binding properties were comparable in all three assays; however, some mutants exhibited marked differences in their ability to bind either 1 M or 3 M. Titres for yeast agglutination was the highest dilution at which agglutination still occurred. The adhesion of mutant E. coli to 1 M and 3 M was assessed, and the raw numbers of binding E. coli were normalised (norm) against E. coli numbers obtained in the same experiment with MSC95-FimH. Data represent mean % (range: lower limit %–upper limit %,). MBP: Mannose binding pocket; 1 M: D-mannose-BSA; 3 M: RNase containing 3-mannose residues; NA: no agglutination. An asterisk (*) indicates that the strains had dysmorphic fimbriae