1887

Abstract

Summary

The ability of pig alveolar macrophages to phagocytose HK 361, which produces both haemolysin II (Apxlll) and pleurotoxin (Apxlll), has been studied. Macrophages incubated with HK 361 in the presence of normal pig serum were rapidly killed. Incubation of the macrophages with a haemolysin-deficient mutant (HK 361 e), which possesses only cytotoxic activity (Apxlll), also caused gross damage to the macrophages. A mutant (HK 361 h) which produces neither Apxll nor Apxlll in its culture supernatant allowed longer survival of the macrophages than did either the parent strain or mutant e when incubated with normal pig serum. Prolonged incubation with mutant h resulted in an increase in the number of damaged macrophages, but not to the same extent as with either HK 361 or mutant e. The number of mutant h cells phagocytosed in the presence of normal pig serum was low. The addition of either hyperimmune rabbit serum, raised against whole formalin-treated HK 361 cells, or convalescent pig serum from a pig recovering from a serotype 3 infection, which contained antibody against both Apxll and Apxlll, did not increase the survival of macrophages incubated with either HK 361 or mutant e. However, incubation of mutant h with convalescent pig serum did result in damage-free macrophages. This serum, which possessed neutralizing capabilities against the toxic activities of Apxll and Apxlll, enhanced the number of mutant h cells phagocytosed compared to the numbers phagocytosed in normal pig serum. Killed bacteria were rapidly phagocytosed and did not damage macrophages. The number of phagocytosed killed bacteria appeared to be similar to that seen with live mutant h cells when incubated in the presence of convalescent pig serum. The presence of a toxic activity associated with the haemolysin-and cytotoxin-negative mutant may represent an additional cell-associated toxin which is not present in its culture supernatant. It appears therefore, that in the absence of extracellular Apxll and Apxlll and in the presence of convalescent pig serum is readily phagocytosed.

Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-140-2-237
1994-02-01
2024-04-23
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/2/mic-140-2-237.html?itemId=/content/journal/micro/10.1099/13500872-140-2-237&mimeType=html&fmt=ahah

References

  1. Bendixen P. H., Shewen P. E., Rosendal S., Wilkie B. N. Toxicity of Haemophilus pleuropneumoniae for porcine lung macrophages, peripheral blood monocytes, and testicular cells. Infect Immun 1981; 33673–676
    [Google Scholar]
  2. Cruikshank R. Mackie & McCartney’s Handbook of Bacteriology.A Guide to Eaboratory Diagnosis and Control of Infection 1962 Edinburgh & London: E. & S. Livingstone.;, 10th edn.313–332
    [Google Scholar]
  3. Cullen J. M., Rycroft A. N. Identification and cross reactivity of the haemolysin and cytotoxin proteins of Actinobacillus pleuropneumoniae and related pathogens by the use of monoclonal antibodies. Proc Int Pig Vet Soc Congr 1992; 12198
    [Google Scholar]
  4. Frey J., Nicolet J. Hemolysin patterns of Actinobacillus pleuropneumoniae. J Clin Microbiol 1990; 28232–236
    [Google Scholar]
  5. Frey J., van den Bosch H., Segers R., Nicolet J. Identification of a second hemolysin (Hlyll) in Actinobacillus pleuropneumoniae serotype 1 and expression of the gene in Escherichia coli. Infec Immun 1992; 601671–1676
    [Google Scholar]
  6. Frey J., Bosse J. T., Chang Y.-F., Cullen J. M., Fenwick B., Gerlach G. F., Gygi D., Haesebrouck F., Inzana T. J., Jansen R., Kamp E. M., Macdonald J., Maclnnes J. I., Mittal K. R., Nicolet J., Rycroft A., Segers R. P. A. M., Smits M. A., Stenbaek E., Struck D. K., van den Bosch J. F., Willson P. J., Young R. Actinobacillus pleuropneumoniae RTX-toxins uniform designation of haemolysins, cytolysins, pleurotoxin and their genes. J Gen Microbiol 1993; 1391723–1728
    [Google Scholar]
  7. Harlow E., Lane D. 1988; Antibodies: a Laboratory Manual. Cold Spring Harbor NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  8. Inzana T. J., Ma J., Workman T., Gogolewski R. P., Anderson P. Virulence properties and protective efficiency of the capsular polymer of Haemophilus (Actinobacillus) pleuropneumoniae serotype 5. Infect Immun 1988; 561880–1889
    [Google Scholar]
  9. Kamp E. M., Popma J. K., Anakotta J., Smits M. A. Identification of hemolytic and cytotoxic proteins of Actinobacillus pleuropneumoniae by use of monoclonal antibodies. Infect Immun 1991; 593079–3085
    [Google Scholar]
  10. Kume K., Nakai T. Species specificity of Haemophilus pleuropneumonia hemolysin demonstrated in the cytocidal and antiphagocytic effects. Jpn J Vet Sri 1986; 48993–997
    [Google Scholar]
  11. Lalonde G., McDonald T. V., Gardner P., O’Hanley P. D. Identification of a hemolysin from Actinobacillus pleuropneumoniae and characterisation of its channel properties in planar phospholipid bilayers. J Biol Chem 1989; 26413559–13564
    [Google Scholar]
  12. Leijh P. C. J., Van Furth R., Van Zwet T. L. 1986; In vitro determination of phagocytes and intracellular killing by polymorphonuclear and mononuclear phagocytes. In Handbook of Experimental Immunology vol. 2, Cellular Immunology, 4th edn.46.1–46.21 Edited by Weir D. M. Oxford: Blackwell Scientific Publications;
    [Google Scholar]
  13. Loftager M. K., Eriksen L., Nielsen R. Antibodies against Actinobacillus pleuropneumoniae serotype 2 in mucosal secretions and sera of infected pigs as demonstrated by an enzyme-linked immunosorbent assay. Res Vet Sri 1993; 5457–62
    [Google Scholar]
  14. Macdonald J., Rycroft A. N. Molecular cloning and expression ofptxA, the gene encoding the 120-kilodalton cytotoxin of Actinobacillus pleuropneumoniae serotype 2. Infect Immun 1992; 602726–2732
    [Google Scholar]
  15. Nakai T., Sawata A., Kume K. Characterization of the hemolysin produced by Haemophilus pleuropneumoniae. Am J Vet Res 1983; 44344–347
    [Google Scholar]
  16. Nicolet J. Haemophilus infections. In Diseases of Swine 1992 Edited by Leman A. D., Straw B., Glock R. D., Mengeling W. L., Penny R. H. C., Scholl E. Ames: Iowa State University Press; pp 426–433
    [Google Scholar]
  17. Pijoan C. Effects of Pasteurella multocida and Haemophilus pleuropneumonia toxins on swine alveolar macrophages. Vet Immunol Immunopathol 1986; 13141–149
    [Google Scholar]
  18. Roberts R. B. The interaction in vitro between group B meningococci and rabbit polymorphonuclear leukocytes, Demon-stration of type specific opsonins and bactericidins. T Exp Med 1967; 126795–799
    [Google Scholar]
  19. Rosendal S., Mitchell W. R., Weber M., Wilson M. R., Zaman M. R. Hemophilus pleuropneumonia lung lesions induced by sonicated bacteria and sterile culture supernatant. Proc Int Pig Vet Soc Congr 1980; 5221
    [Google Scholar]
  20. Rosendal S., Devenish J., Maclnnes J. I., Lumsden J. H., Watson S., Xun H. Evaluation of heat-sensitive, neutrophil-toxic, and hemolytic activity of Actinobacillus (Haemophilus) pleuropneumoniae. Am J Vet Res 1988; 491053–1058
    [Google Scholar]
  21. Rycroft A. N., Cullen J. M. Complement resistance in Actinobacillus (Haemophilus) pleuropneumoniae infection in swine. Am J Vet Res 1990; 511449–1453
    [Google Scholar]
  22. Rycroft A. N., Thompson G., Hammond S. M. The role of cell surface polysaccharide antigens in the pathogenicity of Escherichia coli. FEMS Microbiol Eett 1983; 1849–53
    [Google Scholar]
  23. Rycroft A. N., Williams D., Cullen J. M., Macdonald J. The cytotoxin of Actinobacillus pleuropneumoniae (pleurotoxin) is distinct from the haemolysin and is associated with a 120 kDa polypeptide. J Gen Microbiol 1991; 137561–568
    [Google Scholar]
  24. Sebunya N. K., Saunders J. R. Haemophilus pleuropneumoniae infection in swine: a review. Am J Vet Res 1983; 1821331–1337
    [Google Scholar]
  25. Smits M. A., Briaire J., Jansen R., Smith H. E., Kamp E. M., Gielkens A. L. J. Cytolysins of Actinobacillus pleuropneumoniae serotype 9. Infect Immun 1991; 594497–4504
    [Google Scholar]
  26. Thwaits R. N., Kadis S. Immunogenicity of Actinobacillus pleuropneumoniae outer membrane proteins and enhancement of phagocytosis by antibodies to the proteins. Infect Immun 1991; 59544–549
    [Google Scholar]
  27. Udeze F. A., Kadis S. Effects of Actinobacillus pleuropneumoniae hemolysin on the viability and function of porcine phagocytes. Proc Int Pig Vet Soc Congr 1988; 34
    [Google Scholar]
  28. Udeze F. A., Kadis S. Effects of Actinobacillus pleuropneumoniae hemolysin on porcine neutrophil function. Infect Immun 1992; 601558–1567
    [Google Scholar]
  29. Van Leengoed L. A., Kamp E. M., Pol J. M. A. Toxicity of Haemophilus pleuropneumoniae to porcine lung macrophages. Vet Microbiol 1989; 19337–349
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-140-2-237
Loading
/content/journal/micro/10.1099/13500872-140-2-237
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error