Linker insertion analysis of the FimH adhesin of type 1 fimbriae in an Escherichia coli fimH-null background

Mark Schembri, Lars Pallesen, Hugh Connell, David Hasty, Per Klemm

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The gene encoding the Escherichia coli FimH adhesin has been subjected to linker insertion mutagenesis. Amino acid changes were introduced in a number of positions spanning the entire sequence in order to probe the structure-function relationship of the FimH protein. The effect of these mutations on the ability of bacteria to express a D-mannose binding phenotype was assessed in a fimH null mutant (MS4) constructed by allelic exchange in the E. coli K-12 strain PC31. Mutations mapping at amino acid residues 36, 58, and 279 of the mature FimH protein were shown to completely abolish binding to D-mannose receptors. Differences in the level of fimbriation were also observed as a result of some of the mutations in the fimH gene. These mutants may prove useful in dissecting receptor-ligand interactions by defining regions of the FimH protein that are important in erythrocyte binding.
Original languageEnglish
JournalF E M S Microbiology Letters
Pages (from-to)257-263
Publication statusPublished - 1996

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