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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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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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Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
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The Influence of Human IgG Subclass and Allotype on Complement Activation.

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Structural variations in immunoglobulin G (IgG) allotypes significantly impact complement activation and complement-dependent cytotoxicity (CDC). Specific IgG2 variants and differences between IgG1 and IgG3 subclasses influence cell lysis, offering insights for therapeutic antibody design.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Complement activation via the classical pathway is initiated by C1 binding to oligomeric immunoglobulins (Igs) on target surfaces.
  • Antibody (Ab) structure, including isotype, subclass, and glycosylation, influences complement system activation.
  • Polymorphic variants of IgG can affect Fc-dependent effector functions.

Purpose of the Study:

  • To assess complement binding, deposition, and complement-dependent cytotoxicity (CDC) of 27 known IgG allotypes with anti-trinitrophenyl specificity.
  • To investigate the impact of structural variations within IgG subclasses on complement activation.
  • To elucidate the context-dependent nature of antibody-mediated CDC.

Main Methods:

  • Evaluation of complement binding and deposition across 27 IgG allotypes.
  • Assessment of complement-dependent cytotoxicity (CDC) using various cell lines (human RBCs, Ramos, Raji, Wien133).
  • Comparison of IgG1 and IgG3 subclasses under varying antigen density and in the presence/absence of complement regulators.

Main Results:

  • Minor differences in complement activation were observed among IgG1, IgG3, and IgG4 allotypes, with more substantial variations in IgG2.
  • Allelic variant IGHG2*06 demonstrated reduced complement activation and CDC compared to other IgG2 polymorphisms.
  • Cell lysis varied between IgG1 and IgG3, with IgG3 showing superior lysis of RBCs and Ramos cells, while IgG1 was more effective against Raji and Wien133 cells.
  • Antigen density and antibody hinge length, rather than complement regulators, determined the context-dependent CDC activity of IgG1 and IgG3.

Conclusions:

  • Single amino acid changes and hinge length differences in IgG allotypes can alter their capacity to activate complement.
  • These variations may provide new insights into susceptibility to infectious, alloimmune, and autoimmune diseases.
  • Understanding these structural-functional relationships can aid in the design of improved antibody-based therapeutics.