1887

Abstract

Summary

Several strains were examined for their ability to produce extracellular enzymes that cleave immunoglobulin A and G (Ig A and Ig G) molecules. Two strains isolated from human pulmonary and genital infections produced proteases that cleaved human IgA and IgG, colostral IgA and human myeloma IgA1 and IgA2. Human IgM was not degraded by these enzymes. Examination of cleavage digests showed two main fragments with different electrophoretic mobilities. The two strains produced a protease that cleaved IgA and IgG heavy chains outside the hinge region, and differed in this respect from the hinge-cutting proteases of other bacteria. Protease production may be a virulence mechanism for strains.

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1992-08-01
2022-05-28
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References

  1. Abraham S. N., Beachey E. H. Host defenses against adhesion of bacteria to mucosal surface. In Gallin J. I., Franci A. S. (eds) Advances in host defense mechanisms New York: Raven Press; 198563–88
    [Google Scholar]
  2. William R. C., Gibbons R. J. Inhibition of bacterial adherence by secretory immunoglobulin A: a mechanism of antigen disposal. Science 1972; 177:697–699
    [Google Scholar]
  3. Kilian M., Mestecky J., Schrohenloher R. E. Pathogenic species of the genus Haemophilus and Streptococcus pneumoniae produce immunoglobulin A1 protease. Infect Immun 1979; 26:143–149
    [Google Scholar]
  4. Male C. J. Immunoglobulin A1 protease production by Haem ophilus influenzae and Streptococcus pneumoniae. Infect Immun 1979; 26:254–261
    [Google Scholar]
  5. Plaut A. G., Gilbert J. V., Artenstein M. S., Capra J. D. Neisseria gonorrhoeae and Neisseria meningitidis: extracellular enzyme cleaves human immunoglobulin A. Science 1975; 190:1103–1105
    [Google Scholar]
  6. Plaut A. G. The Ig A1 proteases of pathogenic bacteria. Annu Rev Microbiol 1983; 37:603–622
    [Google Scholar]
  7. Milazzo F. H., Delisle G. J. Immunogobulin A proteases in gram negative bacteria isolated from human urinary tract infections. Infect Immun 1984; 43:11–13
    [Google Scholar]
  8. Molla A., Kagimoto T., Maeda H. Cleavage of immunoglobulin G (IgG) and IgA around the hinge region by proteases from Serratia marcescens . Infect Immun 1988; 56:916–920
    [Google Scholar]
  9. Senior B. W., Albrechtsen M., Kerr M. A. A survey of IgA protease production among clinical isolates of Proteeae . J Med Microbiol 1988; 25:27–31
    [Google Scholar]
  10. Weber D. J., Wolfson J. S., Swartz M. N., Hooper D. C. Pasteurella multocida infections. Report of 34 cases and review of the literature. Medicine 1984; 63:133–154
    [Google Scholar]
  11. Avril J. L., Donnio P. Y., Pouedras P. Selective medium for Pasteurella multocida and its use to detect oropharyngeal carriage in pig breeders. J Clin Microbiol 1990; 28:1438–1440
    [Google Scholar]
  12. Beyt B. E., Sondag J., Roosevelt T. S., Bruce R. Human pulmonary pasteurellosis. JAMA 1979; 242:1647–1648
    [Google Scholar]
  13. Kornfeld S. J., Plaut A. G. Secretory immunity and the bacterial IgA proteases. Rev Infect Dis 1981; 3:521–534
    [Google Scholar]
  14. Avril J. L., Donnio P. Y. Caractérisation des Pasteurella isolées chez l’homme. Pathol Biol 1987; 35:169–172
    [Google Scholar]
  15. Mutters R., Ihm P., Pohl S., Frederiksen W., Mannheim W. Reclassification of the genus Pasteurella Trevisan 1887 on the basis of deoxyribonucleic acid homology, with proposals for the new species Pasteurella dagmatis, P canis, P stomatis, P anatis and P langaa . Int J Syst Bacteriol 1985; 35:309–322
    [Google Scholar]
  16. Carter G. R., Subronto P. Identification of type D strains of Pasteurella multocida with acriflavin. Am J Vet Res 1975; 34:293–294
    [Google Scholar]
  17. Bunn-Moreno M. M., Campos-Neto A. Lectin(s) extracted from seeds of Artocarpus integrifolia (jackfruit): potent and selective stimulator(s) of distinct human T and B cell functions. J Immunol 1981; 127:427–429
    [Google Scholar]
  18. Andre P. M., Le Pogamp P., Chevet D. Impairment of Jacalin binding to serum IgA in IgA nephropathy. J Clin Lab Anal 1990; 4:115–119
    [Google Scholar]
  19. Roque-Barreira M. C., Campos-Neto A. Jacalin: an IgA-binding lectin. J Immunol 1985; 134:1740–1743
    [Google Scholar]
  20. Higerd T. B., Virella G., Cardenas R., Koistinen J. W. New method for obtaining IgA-specific protease. J Immunol Methods 1977; 18:245–249
    [Google Scholar]
  21. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350–4354
    [Google Scholar]
  22. Loomes L. M., Senior B. W., Kerr M. A. A proteolytic enzyme secreted by Proteus mirabilis degrades immunoglobulins of the immunoglobulin A1 (IgA1), IgA2 and IgG isotypes. Infect Immun 1990; 58:1979–1985
    [Google Scholar]
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