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Virion-Associated Cholesterol Regulates the Infection of Human Parainfluenza Virus Type 3

Qiaopeng Tang1, Pengfei Liu2, Mingzhou Chen3

  • 1State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, China. tangqiaopeng@163.com.

Viruses
|May 18, 2019
PubMed

Insights

Human parainfluenza virus type 3 (HPIV3) assembly involves the Fusion (F) protein and occurs in lipid rafts. Cholesterol is crucial for HPIV3 infectivity, suggesting cholesterol disruption as a therapeutic target.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Paramyxovirus matrix (M) proteins are essential for virion assembly and budding.
  • The Fusion (F) protein of Human Parainfluenza Virus Type 3 (HPIV3) plays a key role in viral entry and fusion.
  • Understanding HPIV3 assembly mechanisms is crucial for developing antiviral therapies.

Purpose of the Study:

  • To investigate the assembly mechanism of HPIV3, focusing on the role of the Fusion (F) protein.
  • To characterize the budding process mediated by the HPIV3 F protein.
  • To explore the involvement of lipid rafts and cholesterol in HPIV3 assembly and infectivity.

Main Methods:

  • Expression and characterization of HPIV3 F protein and virus-like particles (VLPs).
  • Construction and recovery of a Flag-tagged HPIV3 recombinant virus (HPIV3F-Flag).
  • Analysis of viral protein and genome localization in lipid rafts using methyl-β-cyclodextrin (MβCD) to deplete cholesterol.

Main Results:

  • HPIV3 F protein expression alone initiates VLP release and regulates M protein VLP-forming ability.
  • M, F, and hemagglutinin-neuraminidase (HN) proteins and the viral genome accumulate in lipid rafts in infected cells.
  • Cholesterol depletion significantly reduces HPIV3 infectivity by impairing viral internalization, indicating HPIV3 assembles in lipid rafts to acquire cholesterol.

Conclusions:

  • HPIV3 assembly likely occurs within lipid rafts, incorporating cholesterol into the viral envelope.
  • The F protein plays a critical role in HPIV3 assembly and VLP formation.
  • Disrupting cholesterol composition in HPIV3 virions presents a potential therapeutic strategy against HPIV3 infection.
Keywords:
HPIV3cholesterolfusion proteininternalizationlipid raftsviral assembly

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