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

Schembri, Mark A. ; Pallesen, Lars ; Connell, Hugh LU ; Hasty, David L. and Klemm, Per (1996) In FEMS Microbiology Letters 137(2-3). p.257-263
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... (More)

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.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
keywords
adhesin, Escherichia coli, FimH, linker insertion mutagenesis, type 1 fimbria
in
FEMS Microbiology Letters
volume
137
issue
2-3
pages
7 pages
publisher
Oxford University Press
external identifiers
  • pmid:8998995
  • scopus:0029900202
ISSN
0378-1097
DOI
10.1016/0378-1097(96)00067-5
language
English
LU publication?
yes
id
fcaf5a40-22a0-4271-afbf-6c35bf879195
date added to LUP
2019-06-19 14:16:44
date last changed
2024-01-30 23:05:16
@article{fcaf5a40-22a0-4271-afbf-6c35bf879195,
  abstract     = {{<p>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.</p>}},
  author       = {{Schembri, Mark A. and Pallesen, Lars and Connell, Hugh and Hasty, David L. and Klemm, Per}},
  issn         = {{0378-1097}},
  keywords     = {{adhesin; Escherichia coli; FimH; linker insertion mutagenesis; type 1 fimbria}},
  language     = {{eng}},
  month        = {{04}},
  number       = {{2-3}},
  pages        = {{257--263}},
  publisher    = {{Oxford University Press}},
  series       = {{FEMS Microbiology Letters}},
  title        = {{Linker insertion analysis of the FimH adhesin of type 1 fimbriae in an Escherichia coli fimH-null background}},
  url          = {{http://dx.doi.org/10.1016/0378-1097(96)00067-5}},
  doi          = {{10.1016/0378-1097(96)00067-5}},
  volume       = {{137}},
  year         = {{1996}},
}