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Related Experiment Videos

Platelet aggregation by group B streptococci.

Y Usui1, Y Ohshima, K Yoshida

  • 1Department of Microbiology, St Marianna University School of Medicine, Kawasaki, Japan.

Journal of General Microbiology
|June 1, 1987
PubMed
Summary
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Certain Group B Streptococcus (GBS) strains, specifically type III, can trigger platelet aggregation. This process is cation-dependent, requires cyclooxygenase activity, and involves bacterial surface components.

Area of Science:

  • Microbiology
  • Hematology
  • Immunology

Background:

  • Group B Streptococcus (GBS) is a significant human pathogen.
  • Platelet aggregation plays a crucial role in hemostasis and thrombosis.
  • The interaction between GBS and platelets is not fully understood.

Purpose of the Study:

  • To investigate the ability of GBS strains to induce platelet aggregation.
  • To characterize the mechanisms involved in GBS-induced platelet aggregation.

Main Methods:

  • Testing 46 GBS strains for platelet aggregation in human platelet-rich plasma.
  • Investigating reaction characteristics including bacterial-to-platelet ratio, cation dependence, cyclooxygenase activity, and serum factor requirements.
  • Assessing platelet lysis and serotonin release.

Related Experiment Videos

  • Evaluating the role of bacterial surface components using antisera and trypsin digestion.

    • Main Results:

    • Four GBS strains, all type III, induced platelet aggregation.
    • Aggregation was maximal at a 4.3 bacteria-to-platelet ratio.
    • The reaction was cation-dependent, required cyclooxygenase activity, and involved fibrinogen and heat-resistant serum factors.
    • GBS induced serotonin release without causing platelet lysis.
    • Type-specific antisera inhibited aggregation with heat-killed bacteria, and trypsin digestion reduced activity.

    Conclusions:

    • Type III GBS possesses the ability to induce platelet aggregation through a mechanism involving bacterial surface components.
    • This interaction is cation-dependent, requires cyclooxygenase activity, and is modulated by serum factors and fibrinogen.
    • Understanding this interaction may offer insights into GBS pathogenesis.