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Related Concept Videos

Antibody Actions01:26

Antibody Actions

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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.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
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Antibody Structure and Classes01:25

Antibody Structure and Classes

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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
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Antibody Structure01:10

Antibody Structure

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Overview
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.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

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An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
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A Kinetic Model of Antigen-Dependent IgG Oligomerization and Complement Binding.

Jürgen Strasser1, Nikolaus Frischauf1, Lukas Schustereder1

  • 1NASAN University of Applied Sciences Upper Austria 4020 Linz Austria.

Small Science
|July 16, 2025
PubMed
Summary

A new kinetic model predicts immunoglobulin G (IgG) oligomer formation, crucial for immune responses and antibody therapies. This understanding aids in optimizing immunotherapies targeting the classical complement pathway (CCP).

Keywords:
C1IgG hexamersIgG oligomerizationIgG subclassesclassical complement pathwaycomplement mediatedkinetic oligomerization modellysis

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Area of Science:

  • Immunology
  • Biophysics
  • Biochemistry

Background:

  • The classical complement pathway (CCP) is vital for immunity, activated by IgG antibody oligomers binding to pathogens or abnormal cells.
  • IgG oligomers also mediate effector functions like antibody-dependent cellular cytotoxicity and phagocytosis via Fcγ receptors.
  • Optimizing IgG-based therapies necessitates a deep understanding of IgG oligomerization dynamics.

Purpose of the Study:

  • To develop a kinetic model predicting IgG oligomer formation.
  • To characterize molecular interactions governing IgG oligomerization.
  • To apply the model for predicting complement-mediated cell lysis.

Main Methods:

  • Development of a kinetic model incorporating IgG concentration, antigen density, subclass, Fc mutants, and inhibitors.
  • Characterization of molecular interactions using single molecule force spectroscopy and grating coupled interferometry.
  • Fitting experimental data from high-speed atomic force microscopy to quantify kinetic and thermodynamic parameters.

Main Results:

  • A predictive kinetic model for IgG oligomer formation was successfully developed.
  • Key rate constants and thermodynamic parameters, including free energy changes, were quantified.
  • The model accurately predicted complement-mediated lysis in liposomal vesicle assays.

Conclusions:

  • The developed mechanistic framework provides insights into IgG oligomerization.
  • This framework can optimize antibody engineering for improved immunotherapies.
  • It also aids in pharmacokinetic/pharmacodynamic modeling for therapies utilizing the CCP.