1887

Abstract

Incubation of either I-labelled or unlabelled with enzymically active preparations of human polymorphonuclear leucocyte lysosomal cathepsin G revealed that surface-exposed outer-membrane proteins were susceptible to proteolytic modification. Electroimmunoblotting experiments confirmed that outer-membrane protein III (PIII) and the major iron-regulated protein (MIRP), two conserved gonococcal proteins, were cleaved by cathepsin G. A direct relationship was observed between susceptibility to the antibacterial properties of cathepsin G and cleavage of PIII among isogenic strains differing in their level of resistance to the bactericidal activity of cathepsin G. Although the antibacterial property of cathepsin G is known to be independent of serine-esterase activity, the data suggest that gonococcal outer-membrane proteins are involved in the binding of cathepsin G, and that variation in the level of resistance reflects the degree to which target outer-membrane proteins such as PIII are exposed.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-133-1-155
1987-01-01
2024-04-24
Loading full text...

Full text loading...

/deliver/fulltext/micro/133/1/mic-133-1-155.html?itemId=/content/journal/micro/10.1099/00221287-133-1-155&mimeType=html&fmt=ahah

References

  1. Blake M. S., Gotschlich E. C., Swanson J. 1981; Effects of proteolytic enzymes on the outer membrane proteins of Neisseria gonorrhoeae. Infection and Immunity 33:212–222
    [Google Scholar]
  2. Bradford M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248–254
    [Google Scholar]
  3. Casey S. G., Shafer W. M., Spitznagel J. K. 1985; Anaerobiosis increases the resistance of Neisseria gonorrhoeae to oxygen-independent antimicrobial cationic proteins of human neutrophil granulocytes. Infection and Immunity 47:40–47
    [Google Scholar]
  4. Casey S. G., Shafer W. M., Spitznagel J. K. 1986; Neisseria gonorrhoeae survive intraleukocytic oxygen-independent antimicrobial capacities of anaerobic and aerobic granulocytes in the presence of pyocin lethal for extracellular gonococci. Infection and Immunity 52:384–389
    [Google Scholar]
  5. Daly J. A., Lee T. J., Spitznagel J. K., Sparling P. F. 1982; Gonococci with mutations to low-level penicillin resistance exhibit increased sensitivity to the oxygen-independent bactericidal activity of human polymorphonuclear leukocyte granule extracts. Infection and Immunity 35:826–833
    [Google Scholar]
  6. Eaton L. J., Rest R. F. 1983; In vivo degradation of gonococcal outer membrane protein within human leukocyte phagolysosomes. Infection and Immunity 42:1034–1040
    [Google Scholar]
  7. Hitchcock P. J. 1984; Analyses of gonococcal lipopolysaccharide in whole cell lysates by sodium dodecyl sulfate-polyacrylamide gel electrophoresis: stable association of lipopolysaccharide with the major outer membrane protein (protein I) of Neisseria gonorrhoeae. Infection and Immunity 46:202–212
    [Google Scholar]
  8. Judd R. C. 1982a; 125I peptide mapping of protein III isolated from four strains of Neisseria gonorrhoeae. Infection and Immunity 37:622–631
    [Google Scholar]
  9. Judd R. C. 1982b; Surface peptide mapping of protein I and protein III of four strains of Neisseria gonorrhoeae. Infection and Immunity 37:632–641
    [Google Scholar]
  10. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
  11. Van der Ley P., Kuipers O., Tommassen J., Lugtenberg B. 1986; O-antigenic chains of lipopolysaccharide prevent binding of antibody molecules to an outer membrane pore protein in Enterobacteriaceae. Microbial Pathogenesis 1:43–49
    [Google Scholar]
  12. Mietzner T. A., Lunginbul G. H., Sandstrom E., Morse S. A. 1984; Identification of an iron- regulated 37,000 dalton protein in the cell envelope of Neisseria gonorrhoeae. Infection and Immunity 45:410–416
    [Google Scholar]
  13. Mietzner T. A., Barnes R. C., JeanLouis Y. A., Shafer W. M., Morse S. A. 1986; Distribution of an antigenically related iron-regulated protein among the Neisseria spp. Infection and Immunity 51:60–68
    [Google Scholar]
  14. Norqvist A., Davies J., Norlander L., Normark S. 1978; The effect of iron starvation on the outer membrane composition of Neisseria gonorrhoeae. FEMS Microbiology Letters 4:71–75
    [Google Scholar]
  15. Odeberg H., Olsson I. 1975; Antibacterial activity of cationic proteins from human granulocytes. Journal of Clinical Investigation 56:1118–1124
    [Google Scholar]
  16. Rest R. F., Cooney M. H., Spitznagel J. K. 1977; Susceptibility of lipopolysaccharide mutants to the bacterial action of human neutrophil lysosome fractions. Infection and Immunity 16:145–151
    [Google Scholar]
  17. Rest R. F., Fisher S. H., Ingham Z. Z., Jones J. J. 1982; Interactions of Neisseria gonorrhoeae with human neutrophils: effects of serum and gonococcal opacity on phagocyte killing and chemiluminescence. Infection and Immunity 36:737–744
    [Google Scholar]
  18. Shafer W. M., Martin L. E., Spitznagel J. K. 1984; Cationic antimicrobial proteins isolated from human neutrophil granulocytes in the presence of diisopropylfluorophosphate. Infection and Immunity 45:29–35
    [Google Scholar]
  19. Shafer W. M., Onunka V. C., Hitchcock P. J. 1986; A spontaneous mutant of Neisseria gonorrhoeae with decreased resistance to neutrophil granule proteins. Journal of Infectious Diseases 153:410–417
    [Google Scholar]
  20. Sparling P. F., Sarubbi F. A. Jr Blackman E. 1975; Inheritance oflow-level resistance to penicillin, tetracycline, and chloramphenicol in Neisseria gonorrhoeae. Journal of Bacteriology 124:740–749
    [Google Scholar]
  21. Spitznagel J. K., Shafer W. M. 1985; Neutrophi1 killing of bacteria by oxygen-independentmechanisms : a historical summary. Reviews of Infectious Diseases 7:398–403
    [Google Scholar]
  22. Spitznagel J. K., Dalldorf F. G., Leffell M. S., Folds J. D., Welsh I. R. H., Cooney M. H., Martin L. E. 1974; Character of azurophil and specific granules purified from human polymorphonuclear leukocytes. Laboratory Investigation 30:774–785
    [Google Scholar]
  23. Swanson J. 1980; Gonococcal growth inhibition and hydrolysis of outer membrane proteins by alpha-chymotrypsin. In Genetics and Immunobiology of Pathogenic Neisseria pp. 19–24 Danielsson D., Normark S. Edited by Umeå: Norrlands-tryck;
    [Google Scholar]
  24. Swanson J., Meyer L. W., Tam M. R. 1982; Antigenicity of Neisseria gonorrhoeae outer membrane proteins(s) III detected by immunoprecipita- tion and Western blot transfer with a monoclonal antibody. Infection and Immunity 38:668–672
    [Google Scholar]
  25. Tam M. R., Buchanan T. M., Sandstrom E. G., Holmes K. K., Knapp J. S., Siadak A. W., Nowinski R. C. 1982; Serological classification of Neisseria gonorrhoeae with monoclonal antibodies. Infection and Immunity 36:1042–1053
    [Google Scholar]
  26. Towbin H., Staehelin T., Gordon J. 1979; Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of the United States of America 76:4350–4354
    [Google Scholar]
  27. Travis T. J., Giles P. J., Porcelli L., Reily C. F., Baugh R., Powers J. 1980; Human leukocyte elastase and cathepsin G: structural and functional characteristics. CIBA Foundation Symposium: Excerpta Medico 75:51–68
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-133-1-155
Loading
/content/journal/micro/10.1099/00221287-133-1-155
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