Receptor-binding function of type 1 pili effects bladder colonization by a clinical isolate of Escherichia coli

Keith, Barry R.; Maurer, Lisa M.; Spears, Patricia A.; Orndorff, Paul E.

doi:10.1128/iai.53.3.693-696.1986

Cited by 86 publications

(34 citation statements)

References 27 publications

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“…This proposition is further supported by epidemiological data (11,47) and by the observation that human urine contains oligosaccharides and Tatnm-Horsfall glycoprotein which are recognized by type 1 fimbriae (33,36) and may inhibit their binding to urinary tract surfaces. It should be noted that the results suggesting a role for type 1 fimbriae in cystitis (1,9,10,17) were obtained with mice and rats. Epithelial cells from urine sediment of rats and humans differ in reactivity with type 1 fimbriae (19).…”

Section: Discussionmentioning

confidence: 98%

“…Our results demonstrate a remarkable tissue tropism for the adhesins in the urinary tract. This obviously relates to the known compartmentation of glycoconjugates along various seg- ments of the nephron (4,(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24). It is also evident that many of the epithelial surfaces of the urinary tract differ in their reactivity with the E. coli adhesins.…”

Section: Discussionmentioning

confidence: 99%

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Binding characteristics of Escherichia coli adhesins in human urinary bladder

et al. 1988

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Binding characteristics of Escherichia coli adhesins in human urinary bladder

et al. 1988

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“…Fimbrial adhesins, such as type 1 fimbriae, play a key role in the attachment of Gram-negative bacteria to the host mucosa (Brinton, 1959;Keith et al, 1986;Sokurenko et al, 1994). In Escherichia coli, type 1 fimbriae are thought to facilitate host-to-host transmission, as well as to be a virulence factor in urinary tract infections (cystitis) (Schaeffer et al, 1987;Connel et al, 1996;Langermann et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Orientational control of fimE expression in Escherichia coli

Sohanpal

Kulasekara

Bonnen

et al. 2001

Molecular Microbiology

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SummaryPhase-variable expression of type 1 fimbriae is, in part, controlled by site-specific DNA inversion of the fim switch in Escherichia coli. Of the two fim recombinases (FimB and FimE) that catalyse the inversion reaction, FimE exhibits a strong bias for phase switching from the ON to the OFF orientation. The specificity associated with fimE is the result of two different mechanisms: (i) FimE exhibits a preference for the invertible element in the ON orientation as substrate for recombination; (ii) the invertible element in the OFF orientation acts in cis to inhibit recombinase activity (orientational control). We show here that the invertible element negatively regulates fimE, even though expression of a fimElacZYA transcriptional fusion is unaffected by orientational control. The fimE transcript extends into the invertible region and hence switch ON-specific and switch OFF-specific mRNA contain different sequences. Furthermore, we show that orientational control is suppressed by the insertion of a structured RNA (tRNA Gly ) between fimE and the fim switch, indicating that the switch OFF-specific mRNA is inactivated by 3 0 to 5 0 degradation. Analysis of the fim switch reveals that it contains two inhibitory elements that exert orientational control independently.

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“…This will also allow us to do site-directed mutagenesis studies to alter these sites. There is a considerable amount of information available in the literature concerning the structure of type 1 pili (20), and the type 1 fimbrial gene clusters of E. coli (22,37) and K. pneumoniae (3) have been cloned. Some interesting studies showed that mutant bacteria lacking the receptor binding function were as ineffective at colonizing the bladder, as were mutants lacking the entire type 1 pili (22).…”

Section: Discussionmentioning

confidence: 99%

Specificity of the high-mannose recognition site between Enterobacter cloacae pili adhesin and HT-29 cell membranes

Pan

Rice

et al. 1997

Infect Immun

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Enterobacter cloacae has been implicated as one of the causative agents in neonatal infection and causes a septicemia thought to be initiated via the gastrointestinal tract. The adhesion of radiolabeled E. cloacae to HT-29 cells was concentration and temperature dependent and was effectively blocked by unlabeled bacteria or by millimolar concentrations of ␣-mannosides and micromolar concentrations of high-mannose oligosaccharides. A variety of well-characterized mannose oligosaccharides were tested as inhibitors of adhesion. The best inhibitor was the Man 9 (GlcNAc) 2-tyrosinamide, which was considerably better than other tyrosinamide-linked oligosaccharides such as Man 7 (GlcNAc) 2 , Man 6 (GlcNAc) 2 or Man 5 (GlcNAc) 2. Further evidence that the bacteria preferred Man 9 (GlcNAc) 2 structures was obtained by growing HT-29 cells in the presence of glycoprotein processing inhibitors that block mannosidase I and increase the amount of protein-bound Man 9 (GlcNAc) 2 at the cell surface. Such cells bound 1.5-to 2-fold more bacteria than did control cells. The adhesin involved in binding to high-mannose structures was purified from isolated pili. On sodium dodecyl sulfate-gels, a 35-kDa protein was identified by its specific binding to a mannose-containing biotinylated albumin. The amino acid sequences of several peptides from the 35-kDa subunit showed over 85% identity to FimH, the mannose-specific adhesin of Salmonella typhimurium. Pili were labeled with 125 I and examined for the ability to bind to HT-29 cells. Binding showed saturation kinetics and was inhibited by the addition of Man 9 (GlcNAc) 2-tyrosinamide but not by oligosaccharides with fewer mannose residues. Polyclonal antibody against this 35-kDa protein also effectively blocked adhesion of pili or E. cloacae, but no effect was observed with nonspecific antibody. These studies demonstrate that the 35-kDa pilus subunit is a lectin whose specificity is directed toward Man 9 (GlcNAc) 2 oligosaccharides.

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Receptor-binding function of type 1 pili effects bladder colonization by a clinical isolate of Escherichia coli

Cited by 86 publications

References 27 publications

Binding characteristics of Escherichia coli adhesins in human urinary bladder

Binding characteristics of Escherichia coli adhesins in human urinary bladder

Orientational control of fimE expression in Escherichia coli

Specificity of the high-mannose recognition site between Enterobacter cloacae pili adhesin and HT-29 cell membranes

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