Examination of Regulatory Cross-talk Between the Decay Accelerating Factor-binding Fimbrial/Afimbrial Adhesins and Type I Fimbriae

Holden, Nicola; Cotterill, Claire; Gally, David L.

doi:10.1007/0-306-46840-9_20

Cited by 4 publications

(3 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These organisms may carry the determinants for several fimbrial and afimbrial adhesins (19). The members of the Afa/Dr family of adhesins, including Dr, Dr-II, AFA I, AFA III, and F1845, have similar genetic organization (32) and recognize DAF as a receptor (31).…”

Section: Discussionmentioning

confidence: 99%

The Afa/Dr Adhesins of Diffusely AdheringEscherichia coliStimulate Interleukin-8 Secretion, Activate Mitogen-Activated Protein Kinases, and Promote Polymorphonuclear Transepithelial Migration in T84 Polarized Epithelial Cells

Bétis

Brest

Hofman³

et al. 2003

Infect Immun

View full text Add to dashboard Cite

Afa/Dr diffusely adhering Escherichia coli (Afa/Dr DAEC) strains cause symptomatic urinary tract and intestinal infections. The proinflammatory effects of Afa/Dr DAEC strains in vitro have been not investigated to date. In the present study, we used confluent polarized monolayers of intestinal cell line T84 to evaluate the consequences of epithelial infection by Afa/Dr DAEC strains in terms of proinflammatory response. Polymorphonuclear leukocyte (PMNL) migration across the epithelial barrier was induced after incubation of the T84 monolayers with the wild-type Afa/Dr DAEC strain C1845 harboring the fimbrial F1845 adhesin and strain IH11128 harboring the Dr hemagglutinin, and the E. coli laboratory strain HB101 was transformed with the pSSS1 plasmid, producing Afa/Dr F1845 adhesin. PMNL migrations were correlated with a basolateral secretion of interleukin-8 by T84 cells and were abolished after incubation of epithelial cells with an anti-decay accelerating factor (DAF) antibody that recognized the short consensus repeat 3 domain of DAF (monoclonal antibody 1H4). Moreover, Afa/Dr DAEC strains induced tyrosine phosphorylation of several T84 proteins and activated the mitogen-activated protein kinases (ERK1/2 mitogen-activated protein, P38, and Jun-C kinases). These data demonstrated for the first time that, in vitro, Afa/Dr DAEC strains exert a proinflammatory signal in intestinal epithelial cells.

show abstract

Section: Discussionmentioning

confidence: 99%

The Afa/Dr Adhesins of Diffusely AdheringEscherichia coliStimulate Interleukin-8 Secretion, Activate Mitogen-Activated Protein Kinases, and Promote Polymorphonuclear Transepithelial Migration in T84 Polarized Epithelial Cells

Bétis

Brest

Hofman³

et al. 2003

Infect Immun

View full text Add to dashboard Cite

show abstract

“…Site-directed mutagenesis introducing a limited number of mutations into the open reading frame, designated daaP, appears to show that a sequence of the DaaP peptide is important and that translation of the daaP gene is required in cis to promote processing by the endonuclease. Interestingly, whereas PapB lowered the level of expression of type 1 fimbriae, DaaA did not (192). Adhesin F1845 has 57% identity with Dr adhesin (91 amino acids out of 160 are identical) (340).…”

Section: Adhesin F1845mentioning

confidence: 99%

Pathogenesis of Afa/Dr Diffusely AdheringEscherichia coli

2005

View full text Add to dashboard Cite

Over the last few years, dramatic increases in our knowledge about diffusely adhering Escherichia coli (DAEC) pathogenesis have taken place. The typical class of DAEC includes E. coli strains harboring AfaE-I, AfaE-II, AfaE-III, AfaE-V, Dr, Dr-II, F1845, and NFA-I adhesins (Afa/Dr DAEC); these strains (i) have an identical genetic organization and (ii) allow binding to human decay-accelerating factor (DAF) (Afa/DrDAF subclass) or carcinoembryonic antigen (CEA) (Afa/DrCEA subclass). The atypical class of DAEC includes two subclasses of strains; the atypical subclass 1 includes E. coli strains that express AfaE-VII, AfaE-VIII, AAF-I, AAF-II, and AAF-III adhesins, which (i) have an identical genetic organization and (ii) do not bind to human DAF, and the atypical subclass 2 includes E. coli strains that harbor Afa/Dr adhesins or others adhesins promoting diffuse adhesion, together with pathogenicity islands such as the LEE pathogenicity island (DA-EPEC). In this review, the focus is on Afa/Dr DAEC strains that have been found to be associated with urinary tract infections and with enteric infection. The review aims to provide a broad overview and update of the virulence aspects of these intriguing pathogens. Epidemiological studies, diagnostic techniques, characteristic molecular features of Afa/Dr operons, and the respective role of Afa/Dr adhesins and invasins in pathogenesis are described. Following the recognition of membrane-bound receptors, including type IV collagen, DAF, CEACAM1, CEA, and CEACAM6, by Afa/Dr adhesins, activation of signal transduction pathways leads to structural and functional injuries at brush border and junctional domains and to proinflammatory responses in polarized intestinal cells. In addition, uropathogenic Afa/Dr DAEC strains, following recognition of β1 integrin as a receptor, enter epithelial cells by a zipper-like, raft- and microtubule-dependent mechanism. Finally, the presence of other, unknown virulence factors and the way that an Afa/Dr DAEC strain emerges from the human intestinal microbiota as a “silent pathogen” are discussed

show abstract

“…Preliminary data suggested that DaaA did not repress type 1 fimbriae (Holden et al ., 2000), and the results here show that the majority of PapB analogues also do not share this specific ability; exceptions being SfaB and PefB that have the highest homology to PapB and were capable of partially repressing type 1 fimbriae expression. The amino and carboxy termini of PapB are unique by comparison with the rest of this regulator family (Fig.…”

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

View full text Add to dashboard Cite

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.

show abstract

Examination of Regulatory Cross-talk Between the Decay Accelerating Factor-binding Fimbrial/Afimbrial Adhesins and Type I Fimbriae

Cited by 4 publications

References 9 publications

The Afa/Dr Adhesins of Diffusely AdheringEscherichia coliStimulate Interleukin-8 Secretion, Activate Mitogen-Activated Protein Kinases, and Promote Polymorphonuclear Transepithelial Migration in T84 Polarized Epithelial Cells

The Afa/Dr Adhesins of Diffusely AdheringEscherichia coliStimulate Interleukin-8 Secretion, Activate Mitogen-Activated Protein Kinases, and Promote Polymorphonuclear Transepithelial Migration in T84 Polarized Epithelial Cells

Pathogenesis of Afa/Dr Diffusely AdheringEscherichia coli

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

Contact Info

Product

Resources

About