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Related Concept Videos

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.
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Antibody Structure01:10

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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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Immunoglobulin-like Cell Adhesion Molecules01:31

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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.
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Diversity of Antigen Receptors01:28

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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.
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Immunocytochemistry and Immunohistochemistry01:22

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Immunocytochemistry (ICC) and immunohistochemistry (IHC) are techniques that use antibodies to check for specific proteins or antigens in a sample. The technique was first published by Albert Coons in 1941 to detect the presence of pneumococcal antigen in tissue sections from mice infected with Pneumococcus. Immunocytochemistry helps localization of proteins or antigens in individual cells like blood cells, stem cells, etc., while immunohistochemistry does the same for tissue samples.
These...
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Immunofluorescence Microscopy01:12

Immunofluorescence Microscopy

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A fluorescence microscope uses fluorescent chromophores called fluorochromes, which can absorb energy from a light source and then emit this energy as visible light. Fluorochromes include naturally fluorescent substances (such as chlorophylls) and fluorescent stains that are added to the specimen to create contrast. Dyes such as Texas red and FITC are examples of fluorochromes. Other examples include the nucleic acid dyes 4’,6’-diamidino-2-phenylindole (DAPI), and acridine orange.
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IgNAR antibody: Structural features, diversity and applications.

Zunera Khalid1, Yulei Chen2, Du Yu3

  • 1Department of Obstetrics and Gynecology, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China.

Fish & Shellfish Immunology
|January 25, 2022
PubMed
Summary

Shark Immunoglobulin Novel Antigen Receptor (IgNAR) antibodies are key to cartilaginous fish immunity. Their unique structure and stability offer significant potential as diagnostic, therapeutic, and research tools.

Keywords:
Cartilaginous fishIgNARNano-bodyTherapeuticsVDJ-RecombinationVNAR

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Area of Science:

  • Immunology
  • Molecular Biology
  • Marine Biology

Background:

  • Cartilaginous fish possess an early humoral immune system utilizing immunoglobulin-type antibodies.
  • Key antibody types in these fish include IgW, IgM, and Immunoglobulin Novel Antigen Receptor (IgNAR).
  • Shark IgNAR antibodies are disulfide-bonded dimers, structurally resembling mammalian IgG heavy chains.

Purpose of the Study:

  • To review the domain characterization, structural features, types, and diversity of shark IgNAR molecules.
  • To highlight the therapeutic applications of IgNAR antibodies.
  • To underscore the potential of IgNAR as a diagnostic, therapeutic, and research tool.

Main Methods:

  • Review of existing literature on shark IgNAR antibodies.
  • Analysis of IgNAR structure, including variable (VNAR) and constant (C1-C5) domains.
  • Examination of VDJ recombination processes and VNAR subclass classification.

Main Results:

  • Shark IgNAR is a primary antibody in adaptive immunity, with serum concentrations of 0.1-1.0 mg/mL.
  • VNARs are classified into subclasses based on non-canonical cysteine residues.
  • VDJ recombination involves four rearrangement procedures to create the complete VNAR repertoire.

Conclusions:

  • IgNAR antibodies possess smaller size, high antigen-binding specificity, and excellent stability.
  • These properties make IgNAR a valuable tool for diagnostics, therapeutics, and research.
  • Further research into IgNAR antibodies is encouraged for their therapeutic potential and role in adaptive immunity.