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Related Experiment Videos

Binding of vitronectin and clusterin by coagulase-negative staphylococci interfering with complement function.

D Q Li1, F Lundberg, A Ljungh

  • 1Department of Medical Microbiology, Dermatology and Infection, Lund University Sölvegatan 23, S-223 62 Lund, Sweden.

Journal of Materials Science. Materials in Medicine
|September 7, 2004
PubMed
Summary

Coagulase-negative staphylococci (CoNS) binding to human vitronectin (Vn) or clusterin (Clu) interferes with complement inhibition. This interaction may promote inflammation around biomaterials during CoNS infections.

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Area of Science:

  • Microbiology
  • Immunology
  • Biomaterials Science

Background:

  • Coagulase-negative staphylococci (CoNS) frequently cause infections on prosthetic devices.
  • Host factors adsorbed on biomaterial surfaces mediate CoNS infections, often triggering inflammation via complement activation.
  • Human vitronectin (Vn) and clusterin (Clu) are complement inhibitors that can be bound by CoNS.

Purpose of the Study:

  • To investigate whether CoNS binding of Vn or Clu influences complement activation.
  • To determine the impact of CoNS-Vn and CoNS-Clu interactions on complement-mediated inflammation.

Main Methods:

  • Complement activation was assessed using a mouse anti-activated human C9 antibody in the presence of Vn.
  • Erythrocyte lysis was measured to evaluate the membrane attack complex formation for Clu.

Related Experiment Videos

  • Experiments involved specific CoNS strains (Staphylococcus hemolyticus SM13I, S. epidermidis 3380, S. epidermidis J9P) and human serum.

    • Main Results:

    • Vn-binding S. hemolyticus SM13I did not alter complement activation on Vn-coated surfaces.
    • Non-Vn-binding S. epidermidis 3380 significantly decreased complement activation on Vn-presented surfaces.
    • Clu-binding S. epidermidis J9P enhanced complement-induced erythrocyte lysis, an effect reduced by exogenous Clu.

    Conclusions:

    • CoNS interaction with Vn and Clu interferes with their complement inhibitory functions.
    • These interactions may disrupt the natural regulation of complement activation.
    • Understanding these interactions is crucial for managing biomaterial-associated CoNS infections.