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Related Experiment Videos

Pattern recognition by TREM-2: binding of anionic ligands.

Michael R Daws1, Paul M Sullam, Eréne C Niemi

  • 1Department of Immunology and Division of Infectious Diseases, Veterans Affairs Medical Center and University of California, San Francisco, CA 94121, USA. mdaws@itsa.ucsf.edu

Journal of Immunology (Baltimore, Md. : 1950)
|July 9, 2003
PubMed
Summary

Researchers identified ligands for triggering receptor expressed by myeloid cells 2 (TREM-2) on bacteria and human astrocytoma cells. TREM-2 recognizes anionic molecules, suggesting a charge-based mechanism for binding both self and pathogen ligands.

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Area of Science:

  • Immunology
  • Molecular Biology

Background:

  • Murine triggering receptor expressed by myeloid cells 2 (TREM-2) is an Ig domain receptor expressed by myeloid cells.
  • TREM-2 plays a role in myeloid cell function and immune responses.

Purpose of the Study:

  • To identify ligands for TREM-2 on bacterial and mammalian cells.
  • To investigate the mechanism of TREM-2 ligand recognition.

Main Methods:

  • Utilized a TREM-2A/IgG1-Fc fusion protein to assess binding to bacteria and cell lines.
  • Employed fluorescently labeled bacteria and reporter assays to study TREM-2 activation.
  • Investigated the role of charge in TREM-2 ligand binding using inhibitory molecules.

Main Results:

  • TREM-2 specifically binds to Gram-negative and Gram-positive bacteria, yeast, and human astrocytoma cells.

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  • Bacterial products like LPS and anionic molecules such as dextran sulfate inhibit TREM-2 binding.
  • TREM-2 activation is induced by bacteria and dextran sulfate, indicating a charge-based recognition mechanism.

    • Conclusions:

    • TREM-2 recognizes anionic ligands on both microbial and mammalian cells, including astrocytomas.
    • The findings suggest a conserved charge-based recognition mechanism for TREM-2, potentially involved in distinguishing self from non-self ligands.