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

Research output: Contribution to journalArticle

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.

Details

Authors
  • Mark A. Schembri
  • Lars Pallesen
  • Hugh Connell
  • David L. Hasty
  • Per Klemm
Organisations
External organisations
  • Technical University of Denmark
  • Danish Serum Institute, Copenhagen
  • University of Tennessee
Research areas and keywords

Keywords

  • adhesin, Escherichia coli, FimH, linker insertion mutagenesis, type 1 fimbria
Original languageEnglish
Pages (from-to)257-263
Number of pages7
JournalFEMS Microbiology Letters
Volume137
Issue number2-3
Publication statusPublished - 1996 Apr 1
Publication categoryResearch
Peer-reviewedYes