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IFN-γ induction on carbohydrate binding module of fungal immunomodulatory protein in human peripheral mononuclear

Yu-Fan Liu1, Shih-Hsien Chang, Hai-Lun Sun

  • 1Department of Biomedical Sciences, Chung Shan Medical University, Taichung 402, Taiwan.

Journal of Agricultural and Food Chemistry
|April 25, 2012
PubMed

Insights

The FIP-fve protein from Flammulina velutipes binds to immune cell surface glycoproteins. This interaction, mediated by its CBM-34 domain, is crucial for FIP-fve

Area of Science:

  • Immunology
  • Biochemistry
  • Mycology

Background:

  • FIP-fve protein from Flammulina velutipes exhibits immunomodulatory effects.
  • Its mechanism of action, particularly receptor interactions, requires elucidation.
  • Known activities include Type II interferon induction and hemagglutination.

Purpose of the Study:

  • To investigate the structural basis of FIP-fve's interaction with immune cells.
  • To determine if the carbohydrate-binding module family 34 (CBM-34) of FIP-fve is conserved.
  • To identify key residues involved in FIP-fve's binding to immune cell surface polysaccharides.

Main Methods:

  • Postulation of three-dimensional structures.
  • Site-directed mutagenesis experiments.
  • Ligand-specific binding competition assays.
  • Treatment of human peripheral mononuclear cells (hPBMCs) with tunicamycin and deglycosylation enzymes.

Main Results:

  • Identified key residues (W24, T28, D34, T90, I91, W111) in FIP-fve's CBM-34 domain crucial for polysaccharide binding.
  • Demonstrated that FIP-fve's CBM-34 domain is conserved.
  • Showed that removal of carbohydrate moieties from hPBMCs reduces IFN-γ induction.

Conclusions:

  • The ligand-binding CBM-34 domain on FIP-fve is essential for its function.
  • Ligand-like glycoproteins on the surface of hPBMCs are required for FIP-fve-induced immunomodulatory effects.
  • This study elucidates the molecular mechanism of FIP-fve's interaction with immune cells.

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