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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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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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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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Development of Immunocompetence01:22

Development of Immunocompetence

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The initiation of cell-mediated immunity can be observed as early as the third month of fetal growth, with active antibody-mediated immunity following approximately one month later.
The initial cells that migrate from the fetal thymus settle within the skin and epithelial tissues lining the mouth, digestive tract, and in females, the uterus and vagina. These cells, including skin-based dendritic cells, serve as antigen-presenting cells, playing a key role in T cell activation.
Subsequent T...
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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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Immunological Memory01:23

Immunological Memory

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Immunological memory, a pivotal pillar of the adaptive immune system, is responsible for the body's ability to remember and respond more swiftly and effectively to previously encountered pathogens. This remarkable feature is what makes vaccines so effective in preventing diseases.
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Related Experiment Video

Updated: Dec 29, 2025

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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Structural insights into immunoglobulin M.

Yaxin Li1,2, Guopeng Wang3, Ningning Li2,3

  • 1State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.

Science (New York, N.Y.)
|February 8, 2020
PubMed
Summary
This summary is machine-generated.

This study reveals the structure of Immunoglobulin M (IgM) complexed with the joining chain (J-chain) and polymeric immunoglobulin receptor (pIgR), clarifying how IgM assembles and is transported for immunity.

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Area of Science:

  • Structural Biology
  • Immunology
  • Molecular Mechanisms

Background:

  • Immunoglobulin M (IgM) is crucial for humoral and mucosal immunity.
  • The assembly and transport of IgM involve the joining chain (J-chain) and polymeric immunoglobulin receptor (pIgR).
  • Molecular mechanisms underlying IgM assembly and transport remain poorly understood.

Purpose of the Study:

  • To elucidate the structural basis of IgM assembly and transport.
  • To determine the molecular interactions between IgM-Fc, J-chain, and pIgR ectodomain.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to visualize the complex.
  • Structural analysis of the human IgM-Fc region in complex with J-chain and pIgR ectodomain.

Main Results:

  • The cryo-EM structure revealed an asymmetric IgM-Fc pentamer with a hexagonal, incomplete triangular formation.
  • IgM-Fc tailpieces form an amyloid-like structure for pentamer stabilization.
  • The J-chain bridges IgM-Fc and pIgR, inducing a significant conformational change in pIgR for complex engagement.

Conclusions:

  • The study provides the first structural insights into the IgM-Fc, J-chain, and pIgR complex.
  • This structural understanding offers a foundation for deciphering the functional mechanisms of IgM in immune responses.