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Hepatitis C Virus RNA-Dependent RNA Polymerase Interacts with the Akt/PKB Kinase and Induces Its Subcellular

María Llanos Valero1, Rosario Sabariegos2, Francisco J Cimas3

  • 1Laboratorio de Virología Molecular, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla-La Mancha, Albacete, Spain.

Antimicrobial Agents and Chemotherapy
|March 30, 2016
PubMed

Insights

Hepatitis C virus (HCV) polymerase NS5B sequesters Akt/protein kinase B (PKB), altering its location. This interaction reveals a new mechanism in HCV infection and potential therapeutic targets.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Hepatitis C virus (HCV) manipulates host cell functions for replication.
  • Akt/protein kinase B (PKB) activation is crucial for HCV entry, but its inactivation during the viral cycle is not fully understood.
  • Viral factors are suspected to cause Akt/PKB inactivation, yet the mechanism remains elusive.

Purpose of the Study:

  • To elucidate the mechanism behind Akt/PKB inactivation during HCV infection.
  • To identify the specific viral component responsible for modulating Akt/PKB activity.
  • To explore the implications of this interaction for novel antiviral strategies.

Main Methods:

  • Expression of HCV polymerase NS5B in cell culture.
  • Analysis of Akt/PKB cellular localization in the presence of NS5B.
  • Investigation in HCV replicon and virus-infected cells.

Main Results:

  • HCV polymerase NS5B directly interacts with Akt/PKB.
  • NS5B alters Akt/PKB's cellular localization from the cytoplasm to the perinuclear region.
  • This NS5B-induced sequestration may explain Akt/PKB's exclusion from early inactivation events.

Conclusions:

  • The interaction between HCV NS5B and Akt/PKB is a novel regulatory step in the HCV life cycle.
  • NS5B-mediated sequestration of Akt/PKB offers a new perspective on HCV pathogenesis.
  • This interaction presents a potential target for developing new anti-HCV therapeutics.

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