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Complement activation by a B cell superantigen

L M Kozlowski1, A M Soulika, G J Silverman

  • 1Division of Allergy and Immunology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|August 1, 1996
PubMed
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Staphylococcal protein A (SpA) binding to VH3+ immunoglobulins (Igs) via its Fab region activates the classical complement pathway. This interaction, independent of Fc binding, generates complement component 3a (C3a).

Area of Science:

  • Immunology
  • Microbial Pathogenesis

Background:

  • Staphylococcal protein A (SpA) is a B cell superantigen that binds to the Fab region of human VH3+ immunoglobulins (Igs).
  • The mechanism by which SpA-Ig interaction triggers complement activation remains incompletely understood.

Purpose of the Study:

  • To investigate whether SpA's interaction with the Fab region of VH3+ Igs initiates complement activation.
  • To determine if this activation proceeds through the classical complement pathway.

Main Methods:

  • Utilized modified SpA (Mod SpA) lacking IgG Fc binding activity.
  • Assessed complement consumption and C3a generation in human serum incubated with Mod SpA.
  • Tested monoclonal IgM proteins for C1q binding after interaction with SpA.
  • Reconstituted hypogammaglobulinemic patient serum with monoclonal IgM proteins to measure complement activation.

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Main Results:

  • Mod SpA induced complement consumption and C3a generation in human serum.
  • C1q binding to SpA was specific to VH3+ IgM proteins that react with SpA.
  • Complement activation and C3a production were observed only when Mod SpA-treated serum was reconstituted with VH3+, SpA-binding IgM proteins.

Conclusions:

  • The interaction between the SpA Fab binding site and VH3+ Igs activates the classical complement pathway.
  • This novel mechanism of complement activation by SpA has potential implications for B cell superantigen activity in vivo.