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Related Concept Videos

Complement System01:27

Complement System

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Methods for Quantitative Detection of Antibody-induced Complement Activation on Red Blood Cells
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Methods for Quantitative Detection of Antibody-induced Complement Activation on Red Blood Cells

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Complement is activated by IgG hexamers assembled at the cell surface.

Christoph A Diebolder1, Frank J Beurskens, Rob N de Jong

  • 1Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, 3584 CH Utrecht, Netherlands.

Science (New York, N.Y.)
|March 15, 2014
PubMed
Summary
This summary is machine-generated.

Antibody Fc interactions form hexamers that activate complement. This discovery provides a model for understanding antibody-mediated complement activation and designing improved antibody therapeutics.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Complement activation by antibodies is crucial for immunity and disease but the mechanism is unclear.
  • Understanding antibody-Fc interactions is key to elucidating complement cascade initiation.

Purpose of the Study:

  • To investigate the mechanism of complement activation by immunoglobulin G (IgG) antibodies.
  • To explore the role of Fc segment interactions in initiating the complement cascade.
  • To develop a model for antibody-mediated complement activation and therapeutic design.

Main Methods:

  • Studied noncovalent interactions between Fc segments of immunoglobulin G (IgG) antibodies.
  • Observed the formation of ordered antibody hexamers upon antigen binding to cells.
  • Investigated the recruitment and activation of C1 (the first complement component) by these hexamers.
  • Manipulated Fc segment interactions across all four human IgG subclasses.

Main Results:

  • Specific noncovalent interactions between IgG Fc segments drive the formation of ordered hexamers after antigen binding.
  • These antibody hexamers effectively recruit and activate C1, initiating the complement cascade.
  • Fc segment interactions can be modulated to control complement activation, including blocking, reconstitution, and enhancement.
  • These findings apply to all four human IgG subclasses, demonstrating a general mechanism.

Conclusions:

  • A novel model for antibody-mediated complement activation via Fc segment-mediated hexamer formation is proposed.
  • This mechanism provides a framework for understanding how antibodies trigger the complement cascade.
  • The findings enable the rational design of antibody-based therapeutics with enhanced efficacy for various applications.