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Related Experiment Videos

Complement S-protein (vitronectin) is associated with cytolytic membrane-bound C5b-9 complexes.

S Bhakdi1, R Käflein, T S Halstensen

  • 1Institute of Medical Microbiology, Max-Planck-Gesellschaft, University of Giessen, FRG.

Clinical and Experimental Immunology
|December 1, 1988
PubMed
Summary

S-protein (vitronectin) binds to cell-associated complement C5b-9 complexes, contrary to prior assumptions. This binding occurs during C9 complex formation, but S-protein’s function remains unclear.

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Area of Science:

  • Immunology
  • Complement System Biology

Background:

  • The complement system is crucial for innate immunity.
  • Terminal complement complexes (C5b-9) mediate cell lysis.
  • S-protein (vitronectin) was thought to only inhibit fluid-phase C5b-9.

Purpose of the Study:

  • To investigate the association of S-protein with cell-bound C5b-9 complexes.
  • To determine if S-protein binds to membrane-inserted C5b-9.
  • To explore the functional implications of S-protein binding to C5b-9.

Main Methods:

  • Monoclonal anti-S-protein antibodies were utilized.
  • Western blot analyses were performed.
  • Sedimentation behavior and co-immunoprecipitation assays were conducted.

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Main Results:

  • S-protein was detected in a fraction of cell-associated C5b-9 complexes.
  • Binding primarily occurs during C9 complex assembly.
  • S-protein did not protect erythrocytes from C5b-9-mediated lysis.
  • Cell-bound S-protein is detectable via immunocytochemistry.

Conclusions:

  • S-protein associates with membrane-bound C5b-9 complexes.
  • The presence of S-protein alone is insufficient to distinguish fluid-phase from membrane-bound C5b-9.
  • The function of cell-associated S-protein requires further investigation.