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Sulfatide negatively regulates the fusion process of human parainfluenza virus type 3

Tadanobu Takahashi1, Kazuhiko Ito, Keijo Fukushima

  • 1Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka and Global COE Program, Shizuoka 422-8526, Japan.

Journal of Biochemistry
|July 24, 2012
PubMed

Insights

Sulfatide, a lipid raft component, plays a role in influenza A virus production. This study reveals sulfatide negatively regulates human parainfluenza virus type 3 (hPIV3) fusion, impacting epithelial cell infection.

Area of Science:

  • Virology
  • Cell Biology
  • Glycosphingolipid Research

Background:

  • Sulfatide (HSO(3)-3-galactosylceramide) is crucial for influenza A virus production in epithelial cells.
  • The role of sulfatide in other viral infections of epithelial cells is largely unknown.

Purpose of the Study:

  • To investigate the effect of sulfatide on human parainfluenza virus type 3 (hPIV3) infection in epithelial cells.
  • To elucidate the mechanism by which sulfatide influences hPIV3 entry and replication.

Main Methods:

  • Utilized genetically engineered sulfatide-enriched cells and sulfatide-deficient cells.
  • Employed virus overlay and solid-phase binding assays to assess hPIV3-sulfatide interaction.
  • Investigated the impact of anti-sulfatide antibody (GS-5) and exogenous sulfatide on hPIV3 infection and syncytia formation.

Main Results:

  • hPIV3 demonstrated binding to sulfatide.
  • Suppression of sulfatide expression reduced hPIV3 infection and multinucleate cell formation.
  • Anti-sulfatide antibody treatment enhanced multinucleate cell formation.
  • Exogenous sulfatide addition reduced multinucleate cell formation in hPIV3-infected cells.

Conclusions:

  • Sulfatide negatively regulates the hPIV3-mediated cell-cell fusion process.
  • This regulation may involve interactions between sulfatide and the hPIV3 hemagglutinin-neuraminidase (HN) or fusion (F) glycoproteins.

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