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Related Concept Videos

Antibody Structure01:10

Antibody Structure

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...
Antibody Structure01:10

Antibody Structure

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...
Antibody Structure and Classes01:25

Antibody Structure and Classes

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.
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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...
Immunoprecipitation01:20

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Antibody Actions01:26

Antibody Actions

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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Related Experiment Video

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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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Duck immunoglobulins: structure, functions and molecular genetics.

D A Higgins1, G W Warr

  • 1Department of Pathology, University of Hong Kong, Queen Mary Hospital, Hong Kong.

Avian Pathology : Journal of the W.V.P.A
|June 1, 1993
PubMed
Summary

Duck immune systems possess four immunoglobulin (Ig) types, including two distinct IgGs. Despite antibody production, ducks often lack key secondary antibody functions due to unique Ig structures.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Veterinary Science

Background:

  • Ducks exhibit four immunoglobulin (Ig) types: IgM, a secretory IgM-like Ig, 7.8S IgG, and 5.7S IgG.
  • The 5.7S IgG is structurally and antigenically similar to an F(ab')2 fragment of the 7.8S IgG.
  • Duck antibody responses follow a sequence: IgM → 7.8S IgG → 5.7S IgG.

Purpose of the Study:

  • Investigate the cellular and molecular events controlling the production of two antigenically related duck IgGs.
  • Understand the structural and functional characteristics of duck immunoglobulins.
  • Clarify the genetic basis for the independent biosynthesis of duck 7.8S and 5.7S IgG heavy chains.

Main Methods:

  • Comparative analysis of immunoglobulin structures.
  • Molecular genetic studies, including cDNA sequencing.
  • Investigation of heavy (H) chain gene locus cloning and sequencing.

Main Results:

  • Duck sera from repeatedly immunized individuals often lack secondary antibody activities (e.g., agglutination, precipitation).
  • Molecular genetic data confirm similarities in VH, CH1, and CH2 domains of 7.8S and 5.7S IgGs.
  • Separate mature messages for heavy chains indicate independent biosynthesis of the two IgGs, with ongoing studies supporting a single-gene hypothesis.

Conclusions:

  • Deficiencies in duck secondary antibody activities may stem from absent functional components in 5.7S IgG or unusual Ig steric structures.
  • Duck IgGs possess an unusual hinge region anatomy and disulfide bond configuration.
  • Further research on duck immunoglobulin structure-function relationships is warranted.