Skip to main content
NCBI home page
Infection and Immunity logoLink to Infection and Immunity
. 1989 Oct;57(10):3210–3213. doi: 10.1128/iai.57.10.3210-3213.1989

Immunoserological comparison of 104-kilodalton proteins associated with hemolysis and cytolysis in Actinobacillus pleuropneumoniae, Actinobacillus suis, Pasteurella haemolytica, and Escherichia coli.

J Devenish 1, S Rosendal 1, R Johnson 1, S Hubler 1
PMCID: PMC260791  PMID: 2674017

Abstract

A homologous polyclonal antibody was produced in a rabbit to the 104-kilodalton (kDa) protein hemolysin of Actinobacillus pleuropneumoniae serotype 1 strain CM-5. In immunoblots, this antibody recognized a similar 104-kDa protein produced in culture supernatants by A. pleuropneumoniae serotypes 1 to 12 and taxon "Minor group" in addition to Pasteurella haemolytica, Actinobacillus suis, and alpha-hemolysin-producing Escherichia coli (but only weakly in the latter two organisms). These results were reproduced by using a mouse monoclonal antibody to the CM-5 104-kDa protein hemolysin, except that the monoclonal antibody bound more strongly to the alpha-hemolysin produced by E. coli, only weakly to the 104-kDa protein produced by "Minor group," and not at all to any extracellular antigens produced by A. suis. Pigs experimentally infected with A. pleuropneumoniae serotypes 1 to 10 and A. suis produced an antibody that recognized the 104-kDa hemolysin produced by CM-5. A pig challenged with a "Minor group" strain did not have such antibodies. Rabbit antiserum produced against the leukotoxin of P. haemolytica and alpha-hemolysin-producing E. coli also recognized the CM-5 hemolysin, but the latter only weakly. The hemolytic activity produced by CM-5 in culture supernatant was neutralized strongly by the pig serum to serotypes 1, 2, 5, 6, 9, and 10 and A. suis, only partially by serotype 8 antiserum and the rabbit antiserum to P. haemolytica leukotoxin, and not all by the antiserum to serotypes 3, 4, and 7 and "Minor group" and the E. coli alpha-hemolysin. These results indicate that a similar but not identical 104-kDa protein is produced in vitro and in vivo by all serotypes of A. pleuropneumoniae and may be related to cytolysins produced by other gram-negative bacteria.

Full text

PDF
3210

Images in this article

3212Image
on p.3212
3212Image
on p.3212
3212Image
on p.3212
3212Image
on p.3212

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benz R., Schmid A., Wagner W., Goebel W. Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates. Infect Immun. 1989 Mar;57(3):887–895. doi: 10.1128/iai.57.3.887-895.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bhakdi S., Mackman N., Nicaud J. M., Holland I. B. Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores. Infect Immun. 1986 Apr;52(1):63–69. doi: 10.1128/iai.52.1.63-69.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Devenish J., Rosendal S. Identification of the heat-labile hemolysin of Actinobacillus pleuropneumoniae serotype 1. Can J Vet Res. 1989 Apr;53(2):251–254. [PMC free article] [PubMed] [Google Scholar]
  4. Eberspächer B., Hugo F., Bhakdi S. Quantitative study of the binding and hemolytic efficiency of Escherichia coli hemolysin. Infect Immun. 1989 Mar;57(3):983–988. doi: 10.1128/iai.57.3.983-988.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Frey J., Nicolet J. Regulation of hemolysin expression in Actinobacillus pleuropneumoniae serotype 1 by Ca2+. Infect Immun. 1988 Oct;56(10):2570–2575. doi: 10.1128/iai.56.10.2570-2575.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Jensen A. E., Bertram T. A. Morphological and biochemical comparison of virulent and avirulent isolates of Haemophilus pleuropneumoniae serotype 5. Infect Immun. 1986 Feb;51(2):419–424. doi: 10.1128/iai.51.2.419-424.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Liggett A. D., Harrison L. R., Farrell R. L. Acute inflammatory effects of intratracheally instilled Escherichia coli endotoxin and sonicated suspension of Haemophilus pleuropneumoniae in swine. Can J Vet Res. 1986 Oct;50(4):526–531. [PMC free article] [PubMed] [Google Scholar]
  8. Lo R. Y., Shewen P. E., Strathdee C. A., Greer C. N. Cloning and expression of the leukotoxin gene of Pasteurella haemolytica A1 in Escherichia coli K-12. Infect Immun. 1985 Dec;50(3):667–671. doi: 10.1128/iai.50.3.667-671.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Maudsley J. R., Kadis S., Mayberry W. R. Isolation, purification, and partial characterization of a lipopolysaccharide from Haemophilus pleuropneumoniae. Infect Immun. 1986 Feb;51(2):501–506. doi: 10.1128/iai.51.2.501-506.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Nielsen R. Haemophilus pleuropneumoniae serotypes--cross protection experiments. Nord Vet Med. 1984 Jul-Aug;36(7-8):221–234. [PubMed] [Google Scholar]
  11. Rosendal S., Boyd D. A., Gilbride K. A. Comparative virulence of porcine Haemophilus bacteria. Can J Comp Med. 1985 Jan;49(1):68–74. [PMC free article] [PubMed] [Google Scholar]
  12. Rosendal S., Devenish J., MacInnes J. I., Lumsden J. H., Watson S., Xun H. Evaluation of heat-sensitive, neutrophil-toxic, and hemolytic activity of Haemophilus (Actinobacillus) pleuropneumoniae. Am J Vet Res. 1988 Jul;49(7):1053–1058. [PubMed] [Google Scholar]
  13. Sebunya T. N., Saunders J. R. Haemophilus pleuropneumoniae infection in swine: a review. J Am Vet Med Assoc. 1983 Jun 15;182(12):1331–1337. [PubMed] [Google Scholar]
  14. Udeze F. A., Latimer K. S., Kadis S. Role of haemophilus pleuropneumoniae lipopolysaccharide endotoxin in the pathogenesis of porcine Haemophilus pleuropneumonia. Am J Vet Res. 1987 May;48(5):768–773. [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES