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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
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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

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The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...
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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.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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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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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.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
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Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay
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Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay

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Diversification of IgG effector functions.

Stylianos Bournazos1, Jeffrey V Ravetch1

  • 1Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065, USA.

International Immunology
|May 5, 2017
PubMed
Summary
This summary is machine-generated.

Immunoglobulin G (IgG) protects the body via its Fab and Fc domains. Fc domain interactions with Fcγ receptors trigger diverse immune responses, crucial for adaptive immunity.

Keywords:
Fc domainFc receptorsantibodiesimmunomodulation

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Immunoglobulin G (IgG) is a key antibody in adaptive immunity.
  • Its bifunctional nature, with antigen-binding Fab domains and effector-mediating Fc domains, is critical for protection.
  • Fc domain interactions with Fc gamma receptors (FcγRs) on leukocytes initiate diverse immunomodulatory pathways.

Purpose of the Study:

  • To explore the diverse effector functions of the IgG Fc domain.
  • To understand how Fc domain structure influences FcγR interactions and downstream signaling.
  • To elucidate the mechanisms of Fc domain-mediated immune modulation.

Main Methods:

  • Analysis of IgG structure-function relationships.
  • Investigation of Fc domain interactions with various Fcγ receptors.
  • Study of Fc-associated glycan structures and IgG subclass variations.

Main Results:

  • Fc effector functions extend beyond phagocytosis and cytotoxicity to include leukocyte modulation, cytokine production, and B-cell regulation.
  • Structural heterogeneity of the IgG Fc domain, including glycan composition and amino acid sequence, dictates FcγR binding affinity.
  • Differential Fc domain phenotypes lead to varied activation of immunomodulatory pathways.

Conclusions:

  • The IgG Fc domain is a versatile mediator of complex immune responses.
  • Structural variations in the Fc domain fine-tune immune activation through distinct FcγR interactions.
  • Understanding Fc domain biology is crucial for developing targeted immunotherapies.