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

FEMS Microbiol Lett. 1996 Apr 1;137(2-3):257-63. doi: 10.1111/j.1574-6968.1996.tb08115.x.

Abstract

The gene encoding the Escherichia coli FimH adhesin of type 1 fimbriae has been subjected to linker insertion mutagenesis. Amino acid changes were introduced at 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / genetics*
  • Adhesins, Bacterial / physiology
  • Adhesins, Escherichia coli*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA Primers / genetics
  • Escherichia coli / genetics*
  • Escherichia coli / physiology
  • Escherichia coli / ultrastructure
  • Fimbriae Proteins*
  • Fimbriae, Bacterial / genetics
  • Fimbriae, Bacterial / physiology
  • Fimbriae, Bacterial / ultrastructure
  • Genes, Bacterial*
  • Guinea Pigs
  • Hemagglutination
  • In Vitro Techniques
  • Microscopy, Electron
  • Molecular Sequence Data
  • Mutagenesis, Insertional
  • Mutation
  • Phenotype

Substances

  • Adhesins, Bacterial
  • Adhesins, Escherichia coli
  • DNA Primers
  • fimH protein, E coli
  • Fimbriae Proteins