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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.
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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Hybridoma Technology01:31

Hybridoma Technology

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Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
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Transcytosis of IgG01:15

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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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Related Experiment Video

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Induction and Assessment of Class Switch Recombination in Purified Murine B Cells
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Antibody Isotype Switching in Vertebrates.

Kate Senger1, Jason Hackney2, Jian Payandeh3

  • 1Department of Immunology, Genentech Inc., South San Francisco, CA, 94080, USA.

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|November 6, 2015
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Antibody isotype switching diversifies immune responses for tissue protection and pathogen clearance. This adaptability is crucial for mucosal immunity, gut homeostasis, and therapeutic applications.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Vertebrate immune systems utilize antibody-mediated responses to combat diverse antigens.
  • Immunoglobulin heavy chain (IgH) isotype switching provides plasticity, enabling antibodies to function in various tissues and bind to Fc receptors and complement.
  • Antibody classes (IgM, IgD, IgG, IgE, IgA) exist in surface-bound and secreted forms, each with distinct roles.

Purpose of the Study:

  • To explore the evolution of antibody isotype switching across species.
  • To provide an overview of the functions of different immunoglobulin isotypes.
  • To emphasize the critical role of IgA in mucosal immunity, gut homeostasis, and pathogen defense.

Main Methods:

  • Review of existing literature on immunoglobulin isotype switching and function.
  • Comparative analysis of isotype evolution in different species.
  • Discussion of IgA's role in mucosal immunity and homeostasis.

Main Results:

  • Isotype switching allows antibodies to maintain antigen specificity while gaining diverse effector functions.
  • Defects in isotype switching are linked to increased susceptibility to infections.
  • High-affinity autoantibodies are implicated in autoimmune diseases like lupus and arthritis.

Conclusions:

  • Secretory IgA antibodies are vital for limiting infections at mucosal surfaces.
  • Mucosal surfaces are key sites for initiating adaptive immune responses, including tolerance to commensals and dietary antigens.
  • Antibodies hold significant potential as therapeutic agents.