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Related Concept Videos

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...
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Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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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.
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Antibody Structure01:10

Antibody Structure

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Transcytosis of IgG01:15

Transcytosis of IgG

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B Cell Activation and Differentiation

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Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance
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Vitellogenin functions as a multivalent pattern recognition receptor with an opsonic activity.

Zhaojie Li1, Shicui Zhang, Qinghui Liu

  • 1Department of Marine Biology, Ocean University of China, Qingdao, People's Republic of China.

Plos One
|April 10, 2008
PubMed
Summary

Fish vitellogenin (Vg) acts as an immune molecule, recognizing pathogens and enhancing macrophage phagocytosis. This reveals a link between reproduction and immunity in fish.

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Published on: March 19, 2010

Area of Science:

  • Immunology
  • Fish Biology
  • Reproductive Biology

Background:

  • Vitellogenin (Vg) is a key reproductive protein in fish.
  • Vg's role in infection resistance is known, but mechanisms are unclear.

Purpose of the Study:

  • To elucidate the mechanisms of Vg's anti-infectious role in fish.
  • To investigate Vg's function as a pattern recognition molecule and opsonin.

Main Methods:

  • Protein-microbe interaction analysis
  • Enzyme-linked immunosorbent assay (ELISA)
  • Phagocytosis assays

Main Results:

  • Fish Vg recognizes bacterial and fungal components, not self-components.
  • Vg functions as an opsonin, enhancing macrophage phagocytosis.
  • Vg exhibits pattern recognition molecule activity with broad specificity.

Conclusions:

  • Fish Vg integrates immune regulation by recognizing pathogen-associated molecular patterns (PAMPs).
  • Vg promotes macrophage phagocytosis, boosting innate immunity.
  • Reproductive proteins like Vg can play dual roles in reproduction and immunity.