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Novel binding between pre-membrane protein and vacuolar ATPase is required for efficient dengue virus secretion

Xiaoqun Duan1, Xi Lu, Jun Li

  • 1Department of Pharmacology, Guilin Medical University, 109 Huancheng Road, Guilin, Guangxi 541004, PR China. robortduan@gmail.com

Biochemical and Biophysical Research Communications
|June 25, 2008
PubMed

Insights

Dengue virus (DV) pre-membrane (prM) protein interacts with vacuolar ATPase (V-ATPase), a host protein crucial for DV entry and egression. This novel interaction reveals V-ATPase

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The flavivirus pre-membrane (prM) protein is essential for envelope (E) protein folding and secretion.
  • Non-structural roles of the prM protein in the viral life cycle remain largely uncharacterized.

Purpose of the Study:

  • To investigate potential interactions between dengue virus (DV) prM protein and host proteins.
  • To determine the role of DV prM protein in viral pathogenesis.

Main Methods:

  • Screening of a human liver cDNA yeast-two-hybrid library to identify interacting host proteins.
  • Analysis of specific amino acid residues in the prM protein crucial for host interaction.
  • Assessing the role of the identified host protein in DV entry and virus egress.

Main Results:

  • Vacuolar ATPase (V-ATPase) was identified as a novel binding partner of DV prM protein.
  • Amino acid residues 76–80 of the prM protein are critical for V-ATPase binding.
  • V-ATPase mediates low-pH dependent entry and influences efficient virus egression.

Conclusions:

  • This study reveals a novel interaction between flavivirus prM protein and V-ATPase.
  • V-ATPase plays a dual role in DV pathogenesis, mediating both viral entry and egression.
  • The prM-V-ATPase interaction is critical for efficient DV replication and spread.

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