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Antigen Presenting Cells01:22

Antigen Presenting Cells

The immune system is a complex network of cells and molecules that protects the body from foreign invaders. T cells, a type of white blood cell, play a crucial role in this process. They recognize and attack foreign substances, such as pathogens, that enter the body.
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An Efficient and High Yield Method for Isolation of Mouse Dendritic Cell Subsets
09:09

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Published on: April 18, 2016

AM3 modulates dendritic cell pathogen recognition capabilities by targeting DC-SIGN.

Diego Serrano-Gómez1, Rocío T Martínez-Nuñez, Elena Sierra-Filardi

  • 1Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.

Antimicrobial Agents and Chemotherapy
|April 25, 2007
PubMed
Summary

The polysaccharide component of AM3 (Inmunoferon) directly interacts with DC-SIGN, a key immune cell receptor. This interaction modulates how dendritic cells recognize pathogens like viruses and fungi.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • AM3 (Inmunoferon) is an oral immunomodulator with largely unknown molecular mechanisms.
  • Dendritic cells (DCs) play a crucial role in initiating immune responses.
  • Lectin-dependent pathogen recognition by DCs is vital for immune surveillance.

Purpose of the Study:

  • To investigate if the polysaccharide moiety of AM3 (IF-S) modulates lectin-dependent pathogen recognition by human dendritic cells.
  • To identify the specific molecular targets of IF-S within dendritic cells.
  • To elucidate the role of DC-SIGN in the immunomodulatory effects of AM3.

Main Methods:

  • Human monocyte-derived dendritic cells and DC-SIGN transfectants were used.
  • Binding assays were performed with various pathogens (viral, fungal, parasitic).
  • DC-SIGN interactions with its counterreceptor (ICAM-3) and HIV gp120 were assessed.
  • DC-SIGN internalization and direct binding of IF-S to DC-SIGN were analyzed using advanced techniques, including NMR.

Main Results:

  • IF-S inhibited the binding of viral, fungal, and parasite pathogens to dendritic cells in a dose-dependent manner.
  • IF-S specifically impaired DC-SIGN-mediated pathogen recognition, including Candida, Aspergillus, and Leishmania.
  • IF-S blocked DC-SIGN interactions with ICAM-3 and HIV gp120, inhibiting HIV capture and trans-infection.
  • IF-S promoted DC-SIGN internalization and directly bound to DC-SIGN on the cell surface.

Conclusions:

  • The polysaccharide moiety of AM3 (IF-S) directly interacts with DC-SIGN, a key receptor on dendritic cells.
  • This interaction modulates dendritic cell pathogen recognition, impacting immune responses.
  • DC-SIGN is identified as a molecular target for AM3, suggesting its immunomodulatory and adjuvant effects are partly mediated through DC-SIGN functional alterations.