1887

Abstract

Summary

The “” (SMG) group have been shown to possess factors that may be involved in pathogenesis. All SMG strains are able to bind fibronectin a cell-surface protein; the binding ranged from 12 to 198 mol/cell. Strains also bound to platelet-fibrin or fibrin clots and fibrinogen, giving maximum adhesion values of 16.5%, 21.8% and 151 mol/cell respectively. Members of the species produced thrombin-like activity. Lancefield group C SMG aggregated rat platelets, a bacterial cell-surface protein acting as mediator in the reaction. Most of the in-vitro factors did not correlate with each other, an indication that SMG strains possess a wide variety of pathogenic properties that may be involved in the production of abscesses or endocarditis. However, there was a correlation between the binding of large amounts of fibrinogen (> 100 mol/cell) and the ability to aggregate platelets. This suggests that fibrinogen binding may aid in platelet aggregation.

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1995-12-01
2024-04-19
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References

  1. Whiley R. A., Hardie J. M. DNA-DNA hybridization studies and phenotypic characteristics of strains within the ‘Streptococcus milleri group’. J Gen Microbiol 1989; 135:2623–2633
    [Google Scholar]
  2. Whiley R. A., Fraser H., Hardie J. M., Beighton D. Phenotypic differentiation of Streptococcus intermedius, Streptococcus constellatus, and Streptococcus anginosus strains within the “Streptococcus milleri group”. J Clin Microbiol 1990; 28:1497–1501
    [Google Scholar]
  3. Whiley R. A., Beighton D. Emended descriptions and recognition of Streptococcus constellatus, Streptococcus intermedius, and Streptococcus anginosus as distinct species. Int J Syst Bacteriol 1991; 41:1–5
    [Google Scholar]
  4. Fisher L. E., Russell R. R. B. The isolation and characterization of milleri group streptococci from dental periapical abscesses. J Dent Res 1993; 72:1191–1193
    [Google Scholar]
  5. Gossling J. Occurrence and pathogenicity of the Streptococcus milleri group. Rev Infect Dis 1988; 10:257–285
    [Google Scholar]
  6. Ruoff K. L. Streptococcus anginosus (“Streptococcus milleri”) : the unrecognized pathogen. Clin Microbiol Rev 1988; 1:102–108
    [Google Scholar]
  7. Drucker D. B., Green R. M. The relative cariogenicities of Streptococcus milleri and other viridans group streptococci in gnotobiotic hooded rats. Arch Oral Biol 1978; 23:183–187
    [Google Scholar]
  8. Mejare B., Edwardsson S. Streptococcus milleri (Guthof); an indigenous organism of the human oral cavity. Arch Oral Biol 1975; 20:757–762
    [Google Scholar]
  9. Piscitelli S. C., Shwed J., Schreckenberger P., Danziger L. H. Streptococcus milleri group: renewed interest in an elusive pathogen. Eur J Clin Microbiol Infect Dis 1992; 11:491–498
    [Google Scholar]
  10. Willcox M. D. P., Knox K. W. Surface-associated properties of Streptococcus milleri group strains and their potential relation to pathogenesis. J Med Microbiol 1990; 31:259–270
    [Google Scholar]
  11. Willcox M. D. P., Patrikakis M., Loo C. Y., Knox K. W. Albumin binding proteins on the surface of the Streptococcus milleri group and characterization of the albumin receptor of Streptococcus intermedius C5. J Gen Microbiol 1993; 139:2451–2458
    [Google Scholar]
  12. Willcox M. D. P., Oakey H. J., Harty D. W. S., Patrikakis M., Knox K. W. Lancefield group C Streptococcus milleri group strains aggregate human platelets. Microb Pat hog 1994; 16:451–457
    [Google Scholar]
  13. Rotstein O. D. Role of fibrin deposition in the pathogenesis of intraabdominal infection. Eur J Clin Microbiol Infect Dis 1992; 11:1064–1068
    [Google Scholar]
  14. Rosenberg M., Gutnick D., Rosenberg E. Adherence of bacteria to hydrocarbons: a simple method for measuring cell-surface hydrophobicity. FEMS Microbiol Lett 1980; 9:29–33
    [Google Scholar]
  15. Unsworth P. F. Hyaluronidase production in Streptococcus milleri in relation to infection. J Clin Pathol 1989; 42:506–510
    [Google Scholar]
  16. Proctor R. A., Christman G., Mosher D. F. Fibronectin-induced agglutination of Staphlococcus aureus correlates with invasiveness. J Lab Clin Med 1984; 104:455–459
    [Google Scholar]
  17. Toy P. T. C. Y., Lai L.-W., Drake T. A., Sande M. A. Effect of fibronectin on adherence of Staphylococcus aureus to fibrin thrombi in vitro. Infect Immun 1985; 48:83–86
    [Google Scholar]
  18. Kuypers J. M., Proctor R. A. Reduced adherence to traumatized rat heart valves by a low-fibronectin-binding mutant of Staphylococcus aureus. Infect Immun 1989; 57:2306–2312
    [Google Scholar]
  19. Lowrance J. H., Baddour L. M., Simpson W. A. The role of fibronectin binding in the rat model of experimental endocarditis caused by Streptococcus sanguis. J Clin Invest 1990; 86:7–13
    [Google Scholar]
  20. Chhatwal G. S., Valentin-Weigand P., Timmis K. N. Bacterial infection of wounds: fibronectin-mediated adherence of group A and C streptococci to fibrin thrombi in vitro. Infect Immun 1990; 58:3015–3019
    [Google Scholar]
  21. Yang K. D., Augustine N. H., Gonzalez L. A., Bohnsack J. F., Hill H. R. Effects of fibronectin on the interaction of polymorphonuclear leukocytes with unopsonized and antibody-opsonized bacteria. J Infect Dis 1988; 158:823–830
    [Google Scholar]
  22. Kluftinger J. L., Kelly N. M., Jost B. H., Hancock R. E. W. Fibronectin as an enhancer of nonopsonic phagocytosis of Pseudomonas aeruginosa by macrophages. Infect Immun 1989; 57:2782–2785
    [Google Scholar]
  23. Manning J. E., Hume E. B. H., Hunter N., Knox K. W. An appraisal of the virulence factors associated with streptococcal endocarditis. J Med Microbiol 1994; 40:110–114
    [Google Scholar]
  24. Finlay-Jones J. J., Hart P. H., Spencer L. K., Nulsen M. F., Kenny P. A., McDonald P. J. Bacterial killing in vitro by abscess-derived neutrophils. J Med Microbiol 1991; 34:73–81
    [Google Scholar]
  25. Gartner T. K., Bennett J. S. The tetrapeptide analogue of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets. J Biol Chem 1985; 260:11891–11894
    [Google Scholar]
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