Genetics of digalactoside-binding adhesin from a uropathogenic Escherichia coli strain

Normark, Staffan; Lark, D; Hull, Richard A.; Norgren, Mari; Båga, Monica; O’Hanley, P; Schoolnik, Gary K.; Falkow, Stanley

doi:10.1128/iai.41.3.942-949.1983

Cited by 169 publications

(59 citation statements)

References 35 publications

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“…Here we show that HB101 contains considerable homology to the type 1 fimbriae genes. We also confirm that P678-54, another strain employed in the analysis of fimbriae (Hull et at.. 1981;Normark et al. 1983;Orndorff and Falkow, 1984;Orndorff efa/., 1965).…”

Section: Introductionsupporting

confidence: 82%

Type 1 fimbriae mutants of Escherichia coli K12: characterization of recognized afimbriate strains and construction of new fim deletion mutants

Blomfield

McClain

Eisenstein

1991

Molecular Microbiology

163

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We have used Southern hybridization analysis to characterize the extent of fim homology in recognized type 1 fimbriae mutants of Escherichia coli K12, including strains HB101, P678-54, and VL584. We have found extensive homology in strain HB101, and confirm that P678-54 lacks the majority of fim DNA. Strain VL584 contains a deletion of the entire fim region. We have used a new allelic exchange procedure to generate novel fim deletion derivatives of strains MG1655, MM294, and YMC9. To increase the utility of the new deletion strains we also isolated recA derivatives of each mutant. These strains facilitate the isolation, characterization, and manipulation of cloned fimbriae genes from diverse sources.

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Section: Introductionsupporting

confidence: 82%

Type 1 fimbriae mutants of Escherichia coli K12: characterization of recognized afimbriate strains and construction of new fim deletion mutants

Blomfield

McClain

Eisenstein

1991

Molecular Microbiology

163

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“…Unlike gonococcal pilus phase variation, which is correlated with chromosomal rearrangement and leads to the loss of pilin expression sites and pilin synthesis (42), loss ofpiliation in the meningococcus and in some gonococcal isolates may represent a defect in the assembly of pili or the anchoring of assembled pili in the outer membrane. These findings suggest that the meningococcal pilus operon may be functionally analogous to the E. coli Gal-Gal pilus operon (43,44), in which cistrons other than the pilus structural gene are required for the biosynthesis and function of normal pilus filaments.…”

Section: Discussionmentioning

confidence: 94%

Pili of Neisseria meningitidis. Analysis of structure and investigation of structural and antigenic relationships to gonococcal pili.

Stephens¹,

Whitney²,

Rothbard³

et al. 1985

The Journal of Experimental Medicine

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To provide information useful for the design of a pilus vaccine effective for the prevention of both meningococcal and gonococcal disease, the electron microscopic morphology of meningococcal pili and the structural and antigenic relationships of meningococcal pili to gonococcal pili were investigated. Meningococcal pili were 4-6 nm in width, extended 500-6,000 nm from the organism surface, and occurred singly or in bundles composed of 8-10 pili per bundle. Meningococcal pilin varied between 17,250 and 20,600 daltons. Pilin was present in outer membrane preparations of some meningococcal isolates that were nonpiliated by electron microscopic examination. Antibodies to gonococcal pili, cyanogen bromide cleavage fragments of gonococcal pilin, or synthetic peptide analogues corresponding to regions of the gonococcal pilin sequence, were used to detect common meningococcal and gonococcal antigenic determinants that might indicate the existence of a conserved sequence beyond residue 29. Antibody to intact gonococcal pili or to the variable CNBR-3 region of gonococcal pilin detected little shared antigenicity with meningococcal pilin. However, pilin from all tested meningococcal isolates reacted with antibody to the CNBR-2 fragment of gonococcal pilin, a region highly conserved among gonococcal strains. Meningococcal pilins were also broadly crossreactive with antibody to a synthetic peptide corresponding to residues 69-84 of the gonococcal sequence, a part of the CNBR-2 region that appears to be critical for gonococcal receptor-binding function. If a sequence similar to 69-84 is also important for receptor-binding function in meningococcal pili, a peptide corresponding to this region may elicit antibodies that block the adherence function of pili elaborated by both Neisseria gonorrhoeae and N. meningitidis.

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“…Similarly, the expression of P-pili is repressed at 25°C in wild-type E, coti but derepressed in an hns mutant (Gbransson etat., 1990). Unlike YMel-2, neither YMel nor ORN125 expresses P-pili from the wild-type operon cloned on pPAP5 (Normark et al. 1983) expression of curli and fibronectin binding may require the RpoS sigma factor which is known to be essential for the expression of a number of stationary-phase-induced genes (Lange and Hengge-Aronis, 1991).…”

Section: Resultsmentioning

confidence: 99%

The RpoS Sigma factor relieves H‐NS‐mediated transcriptional repression of csgA, the subunit gene of fibronectin‐binding curli in Escherichia coli

Olsén

Arnqvist

Hammar

et al. 1993

Molecular Microbiology

265

256

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Curli encoded by the curlin subunit gene, csgA, are fibronectin- and laminin-binding fibres expressed by many natural Escherichia coli and E. coli K-12 strains in response to low temperature, low osmolarity and stationary-phase growth conditions. Curli expression is dependent on RpoS, a sigma factor that controls many stationary phase-inducible genes. Many commonly used K-12 strains carry an amber mutation in rpoS. Strains able to form curli carry an amber suppressor whereas curli-negative E. coli K-12 strains, in general, are sup0. Introduction of SupD, SupE, or supF suppressors into sup0 strains resulted in expression of temperature-regulated curli. In curli-deficient, RpoS- E. coli K-12 strains, csgA is transcriptionally activated by mutations in hns, which encodes the histone-like protein H-NS. Curli expression, fibronectin binding, and csgA transcription remain temperature- and osmoregulated in such double mutants. Our data suggest that RpoS+ strains, and hence curli-proficient strains of E. coli K-12, are relieved for the transcriptional repression mediated by the H-NS protein upon accumulating RpoS as cells reach stationary phase.

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Genetics of digalactoside-binding adhesin from a uropathogenic Escherichia coli strain

Cited by 169 publications

References 35 publications

Type 1 fimbriae mutants of Escherichia coli K12: characterization of recognized afimbriate strains and construction of new fim deletion mutants

Type 1 fimbriae mutants of Escherichia coli K12: characterization of recognized afimbriate strains and construction of new fim deletion mutants

Pili of Neisseria meningitidis. Analysis of structure and investigation of structural and antigenic relationships to gonococcal pili.

The RpoS Sigma factor relieves H‐NS‐mediated transcriptional repression of csgA, the subunit gene of fibronectin‐binding curli in Escherichia coli

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