Sökning: onr:"swepub:oai:lup.lub.lu.se:fcaf5a40-22a0-4271-afbf-6c35bf879195" >
Linker insertion an...
Linker insertion analysis of the FimH adhesin of type 1 fimbriae in an Escherichia coli fimH-null background
-
- Schembri, Mark A. (författare)
- Technical University of Denmark
-
- Pallesen, Lars (författare)
- Danish Serum Institute, Copenhagen,Technical University of Denmark
-
- Connell, Hugh (författare)
- Lund University,Lunds universitet
-
visa fler...
-
- Hasty, David L. (författare)
- University of Tennessee
-
- Klemm, Per (författare)
- Technical University of Denmark
-
visa färre...
-
(creator_code:org_t)
- 1996
- 1996
- Engelska 7 s.
-
Ingår i: FEMS Microbiology Letters. - 0378-1097. ; 137:2-3, s. 257-263
- Relaterad länk:
-
http://dx.doi.org/10...
-
visa fler...
-
https://academic.oup...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- adhesin
- Escherichia coli
- FimH
- linker insertion mutagenesis
- type 1 fimbria
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
Hitta via bibliotek
Till lärosätets databas