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Related Concept Videos

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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Antibody Structure and Classes01:25

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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.
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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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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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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
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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Transcytosis of IgG01:15

Transcytosis of IgG

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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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Determining the Phagocytic Activity of Clinical Antibody Samples
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The Ligands for Human IgG and Their Effector Functions.

Steven W de Taeye1,2, Theo Rispens3, Gestur Vidarsson4

  • 1Sanquin Research, Dept Immunopathology and Landsteiner Laboratory, Amsterdam UMC, University of Amsterdam, 1066 CX Amsterdam, The Netherlands. s.detaeye@sanquin.nl.

Antibodies (Basel, Switzerland)
|September 24, 2019
PubMed
Summary

Antibodies, particularly Immunoglobulin G (IgG), activate immune responses by interacting with effector molecules. Variations in antibody structure and effector molecules influence immune response strength, aiding therapeutic antibody development.

Keywords:
AntibodiesFc effector moleculesIgGallotypesglycosylation

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Humoral immune system activation relies on antibody-antigen recognition and Fc-mediated effector functions.
  • Immunoglobulin G (IgG) is the most prevalent serum antibody isotype, crucial for humoral immune responses.
  • The Fc domain of IgG interacts with various effector molecules, dictating immune response potency.

Purpose of the Study:

  • To provide an overview of IgG interactions with Fc-engaging effector molecules.
  • To discuss how natural variations in antibodies and effector molecules modulate biological activities.
  • To highlight the implications of Fc-mediated effector functions for therapeutic antibody development.

Main Methods:

  • Literature review of IgG-Fc interactions with effector molecules.
  • Analysis of factors influencing IgG-effector molecule binding affinity.
  • Discussion of natural variations impacting antibody effector functions.

Main Results:

  • IgG subclass, allotype, and glycosylation influence Fc-domain interaction strength with effector molecules.
  • Key effector molecules include Fcγ receptors, FcRn, TRIM21, C1, and FcRL receptors.
  • Natural variations on both antibody and effector molecule sides shape antibody biological activities.

Conclusions:

  • Understanding IgG-Fc-mediated effector functions is critical for antibody-based therapies.
  • Knowledge of these interactions informs the development of enhanced therapeutic antibodies for cancer and autoimmune diseases.
  • Variations in antibody and effector molecules provide a basis for fine-tuning immune responses.