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p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha

Christopher O'Connor1, Thomas Pertel, Seth Gray

  • 1Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois, USA.

Journal of Virology
|April 2, 2010
PubMed

Insights

The antiviral protein TRIM5alpha, which blocks retroviral transmission, associates with sequestosome-1/p62. This interaction enhances TRIM5alpha

Area of Science:

  • Virology
  • Immunology
  • Cell Biology

Background:

  • TRIM5 proteins, like TRIM5alpha, restrict retroviral cross-species transmission by binding to viral capsids.
  • TRIM5alpha function is regulated by interferons (IFN), crucial components of the innate immune response.
  • Sequestosome-1/p62 (p62) is an interferon-induced protein involved in cellular signaling pathways that maintain antiviral states.

Purpose of the Study:

  • To investigate the interaction between TRIM5alpha and p62.
  • To determine the functional consequences of this interaction on TRIM5alpha-mediated retroviral restriction.
  • To elucidate the role of p62 in interferon-induced antiviral responses.

Main Methods:

  • Co-localization studies of TRIM5alpha and p62 in cytoplasmic bodies using human and rhesus macaque cell lines.
  • Fluorescence resonance energy transfer (FRET) analysis to confirm protein-protein association.
  • Small interfering RNA (siRNA) to knockdown p62 expression.
  • Assessment of TRIM5alpha protein levels and cytoplasmic body formation.
  • Measurement of TRIM5alpha-mediated retroviral restriction efficiency.

Main Results:

  • p62 co-localizes and directly associates with TRIM5alpha in cytoplasmic bodies.
  • Knockdown of p62 reduces TRIM5alpha protein expression and the formation of TRIM5alpha cytoplasmic bodies.
  • p62 knockdown impairs TRIM5alpha's ability to restrict retroviral infection.
  • These findings suggest p62 enhances TRIM5alpha's antiviral activity.

Conclusions:

  • p62 enhances TRIM5alpha-mediated retroviral restriction, contributing to the interferon-induced antiviral state.
  • The interaction between p62 and TRIM5alpha is a novel mechanism regulating innate antiviral immunity.
  • Targeting the p62-TRIM5alpha interaction could offer new strategies for antiviral therapies.

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