SAP30 deacetylates the Tas protein to inhibit PFV replication

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Using Click Chemistry to Measure the Effect of Viral Infection on Host-Cell RNA Synthesis

Published on: August 9, 2013

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Chenchen Wang1, Junshi Zhang2,3, Yali Xu1

  • 1Key Laboratory of Molecular Microbiology and Technology, College of Life Sciences, Ministry of Education, Nankai University, Tianjin, 300071, China.

Cell & Bioscience
|April 24, 2025
PubMed
Abstract

Insights

SAP30 protein inhibits prototype foamy virus (PFV) replication by deacetylating the Tas protein, which suppresses viral transcription. This discovery sheds light on foamy virus latency.

Area of Science:

  • Virology
  • Molecular Biology
  • Retroviruses

Background:

  • Foamy viruses (FVs) establish lifelong latent infections, hindering research.
  • Studying latent FV infections is crucial due to potential severe consequences from mutations.

Purpose of the Study:

  • Identify host proteins regulating prototype foamy virus (PFV) replication.
  • Investigate the role of SAP30 in PFV infection.

Main Methods:

  • Infection of HT1080 cells with PFV.
  • Transcriptomic sequencing to identify differentially expressed genes.
  • Analysis of SAP30 promoter activity and interaction with Tas protein.
  • Overexpression and knockdown studies of SAP30.
  • Assessment of SAP30's effect on PFV LTR and IP promoter activity.

Main Results:

  • PFV infection upregulates SAP30 mRNA and protein levels.
  • SAP30 inhibits PFV replication; its absence enhances it.
  • SAP30 interacts with Tas protein, leading to its deacetylation.
  • Deacetylation of Tas by SAP30 suppresses PFV transcription.

Conclusions:

  • SAP30 acts as a host restriction factor against PFV.
  • SAP30 inhibits PFV replication via deacetylation of the Tas protein.
  • The C-terminal Sin3 interaction domain of SAP30 is essential for this inhibitory function.
Keywords:
DeacetylationPrototype foamy virusSAP30TasTranscription

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