Virulence of haemolytic strains of<i>Escherichia coli</i>in various animal models

Bosch, J. F. van den; Emödy, Levente; Kétyi, I

doi:10.1111/j.1574-6968.1982.tb08300.x

Cited by 20 publications

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“…The prevalence of hemolytic isolates is 44 to 75% (27,29), whereas only 5 to 15% of normal enteric E. coli strains are hemolytic. Alpha-hemolysin contributes to the severity of experimental pyelonephritis in animal models (10,14,21,30,38,39). Yet the role of alpha-hemolysin antibody in modulating the pathogenic potential of hemolytic strains has not been evaluated critically.…”

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Epitopes of Escherichia coli alpha-hemolysin: identification of monoclonal antibodies that prevent hemolysis

O’Hanley

1990

Infect Immun

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The antigenic regions of Escherichia coli alpha-hemolysin were determined by antibody binding to cyanogen bromide (CnBr) fragments of this protein under denatured conditions. Alpha-hemolysin was isolated from filtered culture supernatants of a recombinant strain by a combination of trichloroacetic acid precipitation and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alpha-hemolysin was used to (i) produce polyclonal rabbit antisera and murine monoclonal immunoglobulin G (IgG) antibodies and (ii) generate CnBr fragments. Rabbit IgG and 13 murine IgG monoclonal antibodies (MAbs) were elicited to alpha-hemolysin as determined by enzyme-linked immunosorbent and immunoprecipitation assays. Antibodies bound to three specific CnBr fragments of alpha-hemolysin in Western blots (immuno-blots) from sodium dodecyl sulfate-polyacrylamide gels: CnBrll (encompassing residues [R] 2 to 160), CnBrV (R 425 to 892), and CnBrVI (R 893 to 1023). Five MAbs bound to CnBrII, seven MAbs bound to CnBrV, and one MAb bound to CnBrVI. These specific CnBr fragments are predicted to be hydrophilic and charged. There was no antibody binding to the highly hydrophobic CnBrlll (R 161 to 416). Similar binding patterns were observed when rabbit polyclonal anti-alpha-hemolysin IgG was used. Polyclonal antibodies to alpha-hemolysin readily inhibited hemolysis and its neutralization capacity was 4-to 64-fold more potent than neutralizing MAbs. The five MAbs that bind to CnBrll possessed hemolytic neutralizing activity to various degrees. In contrast, only three of seven MAbs that bind to CnBrV fragment exhibited neutralization capacity to various degrees; the MAb to CnBrVI did not exhibit this capacity. Based on these data, we predict that denatured alpha-hemolysin and its CnBrII and CnBrV fragments might be worthwhile immunoprophylactic candidates for the prevention of hemolysinmediated E. coli tissue injury.

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Epitopes of Escherichia coli alpha-hemolysin: identification of monoclonal antibodies that prevent hemolysis

O’Hanley

1990

Infect Immun

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“…Haemolytic strains exhibit a high degree of virulence in different animal models whereas nonhaemolytic derivatives obtained either by mutagenesis or plasmid elimination were no longer virulent in the same test systems [7][8][9][10]. Plasmids coding for haemolysin production confer virulence when transferred into suitable nonhaemolytic recipients [7][8][9][10][11]. An isolated chromosomal DNA sequence encoding haemolysin resulted also in enhanced virulence when introduced to a nonhaemolytic faecal isolate of E. coli by recombinant DNA technology [12].…”

Section: Introductionmentioning

confidence: 99%

Transfer of Escherichia coli haemolysin plasmid into Proteus morganii in the mouse intestine

Emödy

1983

FEMS Microbiology Letters

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“…Numerous studies support the idea that alphahaemolysin of Escherichia coli may be a virulence factor in extraintestinal manifestations [1][2][3][4][5][6][7]. Haemolytic strains exhibit a high degree of virulence in different animal models whereas nonhaemolytic derivatives obtained either by mutagenesis or plasmid elimination were no longer virulent in the same test systems [7][8][9][10]. Plasmids coding for haemolysin production confer virulence when transferred into suitable nonhaemolytic recipients [7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transfer of Escherichia coli haemolysin plasmid into Proteus morganii in the mouse intestine

Emödy

Bátai

Kerényi

et al. 1983

FEMS Microbiology Letters

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Virulence of haemolytic strains ofEscherichia coliin various animal models

Cited by 20 publications

References 10 publications

Epitopes of Escherichia coli alpha-hemolysin: identification of monoclonal antibodies that prevent hemolysis

Epitopes of Escherichia coli alpha-hemolysin: identification of monoclonal antibodies that prevent hemolysis

Transfer of Escherichia coli haemolysin plasmid into Proteus morganii in the mouse intestine

Transfer of Escherichia coli haemolysin plasmid into Proteus morganii in the mouse intestine

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