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HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies

Prabhjeet K Phalora1, Nathan M Sherer, Steven M Wolinsky

  • 1Department of Infectious Diseases, Kings College London School of Medicine, Guy's Hospital, London, United Kingdom.

Journal of Virology
|August 24, 2012
PubMed

Insights

APOBEC3 proteins are key in antiviral defense, but P bodies and associated proteins do not regulate HIV-1 replication or APOBEC3 antiviral activity. Localization to P bodies may sequester APOBEC3 activity or link to unknown functions.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • APOBEC3 cytidine deaminases are crucial for host defense against viruses like HIV-1 and endogenous elements.
  • APOBEC3 proteins interact with RNA metabolism factors and localize to P bodies, sites of mRNA decay.

Purpose of the Study:

  • To investigate the role of P bodies and associated proteins in HIV-1 replication.
  • To determine the impact of P bodies on APOBEC3 antiviral activity.

Main Methods:

  • Depletion of P-body components (DDX6, Lsm1) and Argonaute proteins.
  • Assessing HIV-1 replication, APOBEC3 packaging, and infectivity.
  • Investigating colocalization of viral components and P-body proteins.
  • Evaluating APOBEC3 modulation of microRNA activity.

Main Results:

  • Depletion of DDX6 or Lsm1 did not affect HIV-1 replication, APOBEC3 virion packaging, or antiviral activity.
  • HIV-1 genomic RNA and Gag did not colocalize with P-body proteins.
  • Depletion of Argonaute proteins modestly increased viral infectivity.
  • APOBEC3 proteins did not specifically regulate microRNA function.

Conclusions:

  • P bodies and associated proteins do not regulate HIV-1 replication or APOBEC3 antiviral activity.
  • P body localization might sequester APOBEC3 enzymatic activity or be linked to unidentified cellular functions.

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