Linker insertion analysis of the FimH adhesin of type 1 fimbriae in an Escherichia coli fimH-null background
(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
- Schembri, Mark A. ; Pallesen, Lars ; Connell, Hugh LU ; Hasty, David L. and Klemm, Per
- organization
- publishing date
- 1996-04-01
- 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}}, }