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Role of ATP in influenza virus budding

E K Hui1, D P Nayak

  • 1Department of Microbiology, Immunology, and Molecular Genetics, UCLA School of Medicine, Los Angeles, California 90095-1747, USA.

Virology
|March 9, 2002
PubMed

Insights

Influenza virus budding requires ATP hydrolysis, not just binding. Metabolic inhibitors that deplete ATP reduce budding, which is reversible. Membrane viscosity also impacts this critical viral replication step.

Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Influenza virus replication involves budding from host cell plasma membranes.
  • The specific requirements and energy dependence of this budding process remain largely uncharacterized.

Purpose of the Study:

  • To investigate the role of adenosine triphosphate (ATP) and its hydrolysis in influenza virus budding.
  • To explore the influence of membrane biophysical properties on virus budding.

Main Methods:

  • Treatment of infected Madin-Darby canine kidney (MDCK) cells with metabolic inhibitors affecting ATP production.
  • Analysis of ATP hydrolysis requirement using lysophosphatidylcholine-permeabilized cells and non-permeable ATP analogues.
  • Assessment of virus budding rates under varying membrane viscosity conditions using dimethyl sulfoxide (DMSO).

Main Results:

  • Metabolic inhibitors targeting ATP production significantly reduced influenza virus budding in a reversible manner.
  • ATP hydrolysis, but not ATP binding alone, was essential for efficient virus budding.
  • Inhibitors of ion channels and protein ubiquitination did not affect budding, ruling out their direct involvement.
  • Decreased membrane viscosity induced by DMSO treatment also inhibited virus budding.

Conclusions:

  • Influenza virus budding is an active, ATP-dependent process relying on ATP hydrolysis.
  • Membrane biophysical properties, specifically viscosity and fluidity, play a crucial role in regulating virus budding efficiency.

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