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BAY 41-4109-mediated aggregation of assembled and misassembled HBV capsids in cells revealed by electron microscopy

Virgile Rat1, Florian Seigneuret1, Julien Burlaud-Gaillard2

  • 1Morphogenèse et Antigénicité Du VIH et des Virus des Hépatites, Inserm - U1259 MAVIVH, Université de Tours et CHRU de Tours, 10 Boulevard Tonnellé - BP 3223, 37032, Tours Cedex 1, France.

Antiviral Research
|July 15, 2019
PubMed

Insights

The Hepatitis B virus (HBV) core protein (HBc) aggregates in liver cells when treated with BAY 41-4109. This drug candidate causes nuclear envelope deformation and forms capsid-like shells, offering insights into HBV antiviral strategies.

Area of Science:

  • Hepatology
  • Virology
  • Structural Biology

Background:

  • The Hepatitis B virus (HBV) core protein (HBc) is crucial for forming the HBV capsid.
  • HBc's diverse roles in viral replication present it as a key target for antiviral drug development.
  • Previous research identified HBV assembly inhibitors, or capsid assembly modulators, based on HBc structure.

Purpose of the Study:

  • To investigate the effects of BAY 41-4109, a heteroaryldihydropyrimidine derivative, on HBc aggregation and HBV capsid formation.
  • To elucidate the ultrastructural organization of HBc aggregates induced by BAY 41-4109.
  • To understand the mechanism of action of BAY 41-4109 as an HBV antiviral agent.

Main Methods:

  • Confocal microscopy to observe BAY 41-4109-mediated HBc aggregation in Huh7 cells.
  • Image analysis to quantify aggregate size in relation to drug concentration and treatment duration.
  • Transmission electron microscopy (TEM) and immuno-TEM to examine the ultrastructure of HBc aggregates and their interaction with the nuclear envelope.

Main Results:

  • BAY 41-4109 induced HBc aggregation, primarily in the cytoplasm of Huh7 cells.
  • Aggregate size was dose- and time-dependent.
  • Large aggregates were associated with nuclear envelope invaginations, confirmed by TEM.
  • TEM and immuno-TEM revealed aggregates composed of capsid-like shells containing HBV core fragments.

Conclusions:

  • BAY 41-4109 promotes the formation of non-capsid HBc polymers.
  • The drug induces significant ultrastructural changes, including nuclear envelope deformation.
  • These findings provide insights into the mechanism of action of BAY 41-4109 and serve as a reference for other HBV capsid assembly inhibitors.

Keywords:
AggregationCAMsConfocal microscopyElectron microscopyHBVHBc

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