Regulation of production of type 1 pili among urinary tract isolates of Escherichia coli

Hultgren, S.J.; Schwan, William R.; Schaeffer, Anthony J.; Duncan, James L.

doi:10.1128/iai.54.3.613-620.1986

Cited by 192 publications

(80 citation statements)

References 36 publications

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“…Strains were grown statically at 37°C described above to induce type 1 pili production. Haemagglutination assays with guinea pig erythrocytes (Colorado Veterinary Products) were performed following published protocols (Hultgren et al, 1986). Results represent three independent experiments.…”

Section: Haemagglutination Assay For Type 1 Piliationmentioning

confidence: 99%

Development of intracellular bacterial communities of uropathogenicEscherichia colidepends on type 1 pili

Wright

Seed

Hultgren

2007

Cellular Microbiology

296

271

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SummaryUropathogenic Escherichia coli, the predominant causative agent of urinary tract infections, use type 1 pili to bind and invade bladder epithelial cells. Upon entry, the bacteria rapidly replicate and enter a complex developmental pathway ultimately forming intracellular bacterial communities (IBCs), a niche with biofilm-like properties protected from innate defences and antibiotics. Paradoxically, bacteria within IBCs produce type 1 pili, an organelle thought only to be an extracellular colonization factor. Thus, we investigated the function of type 1 pili in IBC development. The cystitis isolate, UTI89, was genetically manipulated for conditional fim expression under control of the tet promoter. In this strain, UTI89-tetR/P tet fim, piliation is constitutively inhibited by the tetracycline repressor, TetR. Repression is relieved by anhydrotetracycline (AHT) treatment. UTI89-tetR/ Ptet fim and the isogenic control strain, UTI89-tetR, grown in the presence of AHT, colonized the bladder and invaded the superficial umbrella cells at similar levels at early times in a murine model of infection. However, after invasion UTI89-tetR/Ptet fim became non-piliated and was unable to form typical IBCs comprised of tightly packed, coccoid-shaped bacteria in contrast to the control strain, UTI89-tetR. Thus, this work changes the extracellular colonization functional paradigm of pili by demonstrating their intracellular role in biofilm formation.

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Section: Haemagglutination Assay For Type 1 Piliationmentioning

confidence: 99%

Development of intracellular bacterial communities of uropathogenicEscherichia colidepends on type 1 pili

Wright

Seed

Hultgren

2007

Cellular Microbiology

296

271

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“…To this end, we transformed a wild-type E. coli strain (MG1655), expressing type 1 fimbria and wild-type FimH, with the plasmids encoding the FimH chimeras. Upon induction of the chimeras, the level of wild-type FimH on the surface of E. coli cells was quantified in a standard haemagglutination assay with guinea pig erythrocytes (Hultgren et al, 1985;1986) using serial twofold dilutions of the cultures. As shown in Table 2, identical haemagglutination indexes (2 8 = 256) were obtained for E. coli MG1655 cells transformed with the empty vector (pVLT35) or with any of the plasmids encoding the FimH chimeras (regardless of being deletion, substitution or fusion chimeras).…”

Section: Fimh Chimeras Do Not Inhibit the Function Of Fimd Ushermentioning

confidence: 99%

Recognition of the N‐terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis

Múnera

Hultgren

Fernández

2007

Molecular Microbiology

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SummaryIn this work we discover that a specific recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is essential for the biogenesis of type 1 pili in Escherichia coli. These filamentous organelles are assembled by the chaperone-usher pathway, in which binary complexes between fimbrial subunits and the periplasmic chaperone FimC are recognized by the outer membrane protein FimD (the usher). FimH adhesin initiates fimbriae polymerization and is the first subunit incorporated in the filament. Accordingly, FimD shows higher affinity for the FimC/FimH complex although the structural basis of this specificity is unknown. We have analysed the assembly into fimbria, and the interaction with FimD in vivo, of FimH variants in which the N-terminal lectin domain of FimH was deleted or substituted by different immunoglobulin (Ig) domains, or in which these Ig domains were fused to the N-terminus of full-length FimH. From these data, along with the analysis of a FimH mutant with a single amino acid change (G16D) in the N-terminal lectin domain, we conclude that the lectin domain of FimH is recognized by FimD usher as an essential step for type 1 pilus biogenesis.

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“…These regulators are (with the associated adhesin gene cluster in parenthesis): sfaB (S), daaA (F1845), faeB (K88), fanA (K99), fanB (K99), clpB (CS31A) and S. enterica serovar Typhimurium pefB (Pef). Type 1 fimbriae are associated with the majority of E. coli pathotypes and fim will be present in most strains that carry these additional adhesins (Buchanan et al, 1985;Hultgren et al, 1986;Leathart and Gally, 1998). P-pili are associated with uropathogenic E. coli, although because of receptor specificity, expression of P-pili is more commonly associated with upper urinary tract infections (Ekback et al, 1986;Svanborg et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

PapB paralogues and their effect on the phase variation of type 1 fimbriae in Escherichia coli

Holden

Uhlin

Gally

2001

Molecular Microbiology

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SummaryRecent work has demonstrated that expression of type 1 fimbriae is repressed by PapB, a regulator of pyelonephritis-associated pili (P-pili). PapB belongs to family of related adhesin regulators, for which consensus residues required for DNA binding and oligomerization have been identified. Of the regulators tested in this study, PapB, SfaB (S-fimbriae) and PefB (Salmonella enterica serovar Typhimuriumplasmid-encoded fimbriae) repressed FimB-promoted off-to-on inversion of the fim switch, although complete repression was only demonstrated by PapB. DaaA, FaeB, FanA, FanB and ClpB had no effect on fim switching. In addition, only PapB stimulated FimE-promoted on-to-off inversion. Deletion analysis demonstrated that this specificity resides in the carboxy terminal of the protein, and not the amino terminal, with the central region being homologous among the family members. Exchange of Leu 82 and Ile 83 of PapB for the equivalent residues from the DaaA protein (Phe and Gln) within the carboxy terminal virtually abolished cross-talk activity. Whereas PapB can bind to a region around the left inverted repeat of the fim switch, DaaA and the PapB double mutant were effectively unable to bind this region. A previously characterized PapB DNA binding mutant also failed to bind to this region and failed to inhibit FimB activity at the fim switch. Thus, repression of fim expression appears unique to PapB and SfaB within E. coli and requires DNA binding involving amino acid residues located both within the homologous core and in the heterogeneous carboxy terminus. The variation in the carboxy terminus between the PapB family members explains their differential effects on fim. This mechanism of cross-talk seems restricted to the P and S family adhesins with type 1 fimbriae and may ensure variable and sequential expression of adhesins during urinary tract infections.

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Regulation of production of type 1 pili among urinary tract isolates of Escherichia coli

Cited by 192 publications

References 36 publications

Development of intracellular bacterial communities of uropathogenicEscherichia colidepends on type 1 pili

Development of intracellular bacterial communities of uropathogenicEscherichia colidepends on type 1 pili

Recognition of the N‐terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis

PapB paralogues and their effect on the phase variation of type 1 fimbriae in Escherichia coli

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