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RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription

Charles-Adrien Richard1, Vincent Rincheval2, Safa Lassoued3

  • 1Unité de Virologie et Immunologie Moléculaires (UR892), INRA, Université Paris-Saclay, Jouy-en-Josas, France.

Plos Pathogens
|March 1, 2018
PubMed

Insights

Respiratory syncytial virus P protein recruits M2-1 to inclusion bodies and facilitates its dephosphorylation via PP1, a crucial step for efficient viral RNA transcription and mRNA binding.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Respiratory syncytial virus (RSV) RNA synthesis is concentrated in cytoplasmic inclusion bodies (IBs).
  • Viral RNA polymerase components aggregate within IBs for efficient replication.
  • The M2-1 protein is an essential transcription factor for RSV.

Purpose of the Study:

  • To investigate the role of the RSV P protein in recruiting and regulating the M2-1 transcription factor.
  • To elucidate the mechanism of M2-1 dephosphorylation and its impact on viral transcription.
  • To identify the interaction sites between P, M2-1, and PP1.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to confirm protein-protein interaction regions.
  • Analysis of M2-1 phosphorylation state in relation to P protein interaction.
  • Assessment of viral transcription efficiency upon disruption of P-PP1 interaction.

Main Results:

  • RSV P protein recruits M2-1 to IBs independently of M2-1 phosphorylation.
  • P forms a complex with cellular phosphatase PP1, enabling M2-1 dephosphorylation.
  • Disruption of the P-PP1 interaction impairs M2-1 dephosphorylation and viral transcription.
  • M2-1 exclusion from IBAGs upon P-PP1 disruption suggests a role in mRNA binding.

Conclusions:

  • M2-1 dephosphorylation, mediated by the P-PP1 complex, is essential for efficient RSV RNA transcription.
  • Dephosphorylated M2-1 is competent for viral mRNA binding, indicating a post-transcriptional role.
  • The P-PP1 interaction is critical for regulating M2-1 function during the RSV replication cycle.

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