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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 Structure01:10

Antibody Structure

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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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Protein Families02:47

Protein Families

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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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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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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
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Comparative functional characterization of canine IgG subclasses.

Lisa M Bergeron1, Erin E McCandless1, Steve Dunham1

  • 1Zoetis, Global Therapeutic Research, Veterinary Medicine Research and Development, 333 Portage Road, Kalamazoo, MI 49007, USA.

Veterinary Immunology and Immunopathology
|November 26, 2013
PubMed
Summary
This summary is machine-generated.

This study characterizes canine IgG subclasses, revealing distinct functional properties. Canine subclasses B and C exhibit antibody-dependent cell-mediated cytotoxicity (ADCC), aiding therapeutic antibody development.

Keywords:
ADCCCDCCDRCanineEffector functionsFc receptorIgG subclassImmunoglobulinantibody-dependent cell-mediated cytotoxicitycell-mediated cytotoxicitycomplementarity determining region

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Area of Science:

  • Immunology
  • Veterinary Medicine
  • Biotechnology

Background:

  • Limited understanding of canine immunoglobulin G (IgG) subclass functions, including complement-dependent cytotoxicity (CDC) and antibody-dependent cell-mediated cytotoxicity (ADCC).
  • Critical knowledge gap for advancing canine immunology and developing canine therapeutic monoclonal antibodies.

Purpose of the Study:

  • To functionally characterize the four published canine IgG subclasses.
  • To determine effector functions, complement binding, FcRn binding, and ADCC capabilities for each subclass.
  • To establish functional parallels between canine and human IgG subclasses for translational applications.

Main Methods:

  • In vitro and ex vivo experiments were conducted to evaluate canine Fc effector functions.
  • Assessment of complement binding, FcRn binding, and ADCC activity for canine IgG subclasses.
  • Characterization of canine Fc fusions, canine chimeras, and caninized antibodies.

Main Results:

  • Canine IgG subclasses A and D were identified as effector-function negative.
  • Canine IgG subclasses B and C demonstrated binding to canine Fc gamma receptors and positive ADCC activity.
  • All canine IgG subclasses, except subclass C, bind the neonatal Fc receptor (FcRn).

Conclusions:

  • Canine IgG subclasses exhibit distinct functional profiles, with subclasses B and C mediating ADCC.
  • The findings provide a functional categorization of canine IgG subclasses, analogous to human IgG subclasses.
  • This research lays the groundwork for canine therapeutic antibody development and enhances understanding of canine immunology.