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Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity

Taisuke Izumi1, Ryan Burdick, Mayu Shigemi

  • 1Viral Mutation Section.

Journal of Virology
|August 9, 2013
PubMed

Insights

Mov10 and APOBEC3G (A3G) inhibit HIV-1 replication and are found in virions. Their antiviral activity and incorporation into virions do not depend on P-body localization, challenging previous assumptions.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Mov10 and APOBEC3G (A3G) are known to localize to processing bodies (P bodies) and inhibit HIV-1 replication.
  • The precise role of P-body localization in the antiviral functions of Mov10 and A3G, including virion incorporation, remains unclear.

Purpose of the Study:

  • To investigate the functional significance of Mov10 and A3G P-body localization for their antiviral activities and virion incorporation.
  • To elucidate the molecular complexes and cellular localization of Mov10 and A3G during HIV-1 replication.

Main Methods:

  • Mutagenesis of Mov10 to assess the role of its helicase domain in P-body localization and antiviral activity.
  • Knockdown of P-body components (DDX6) and other proteins (SRP19, AGO2) to evaluate their impact on Mov10/A3G function.
  • Sucrose gradient sedimentation assays to analyze the molecular mass of Mov10, A3G, and associated viral/cellular factors.

Main Results:

  • A Mov10 helicase mutant showed reduced P-body localization but retained antiviral activity via virion incorporation.
  • Disruption of P bodies did not abolish Mov10's antiviral effects.
  • Mov10 and A3G predominantly form high-molecular-mass (HMM) complexes, distinct from low-molecular-mass (LMM) P-body markers.
  • Virion incorporation and antiviral activity of Mov10 and A3G are independent of P-body localization.

Conclusions:

  • The functional antiviral activities and virion incorporation of Mov10 and A3G are not dependent on their localization to P bodies.
  • Mov10 and A3G exist in distinct high-molecular-mass complexes separate from canonical P-body components.
  • These findings redefine the understanding of Mov10 and A3G's mechanism of HIV-1 inhibition.

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