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Related Experiment Videos

Epstein-Barr virus SM protein

I D Cook1, F Shanahan, P J Farrell

  • 1Ludwig Institute for Cancer Research, St. Mary's Hospital Medical School, London, United Kingdom.

Virology
|November 15, 1994
PubMed
Summary
This summary is machine-generated.

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The Epstein-Barr virus (EBV) SM protein, a key player in viral replication, is a phosphoprotein that transactivates gene expression. Its phosphorylation by casein kinase II (CKII) is crucial, though not essential for transactivation activity.

Area of Science:

  • Virology
  • Molecular Biology
  • Cellular Biology

Background:

  • Epstein-Barr virus (EBV) productive cycle involves complex protein interactions.
  • The BMLF1 open reading frame encodes critical viral proteins.
  • The SM protein is highly abundant during early EBV replication.

Purpose of the Study:

  • To characterize the protein products of the EBV BMLF1 open reading frame.
  • To investigate the role of SM protein phosphorylation in EBV infection.
  • To elucidate the mechanism of transactivation by EBV BMLF1 proteins.

Main Methods:

  • Characterization of EBV protein products in B95-8 and Akata cells.
  • In vitro phosphorylation assays using casein kinase II (CKII).
  • Bioinformatic analysis of protein sequences for homology and phosphorylation sites.

Related Experiment Videos

  • Site-directed mutagenesis to study the effect of CKII site modification.
  • Transient transfection assays with CAT reporter constructs to assess gene transactivation.

    • Main Results:

    • The SM protein, derived from spliced RNA, is the most abundant protein product.
    • SM is a phosphoprotein in EBV-infected cells and is phosphorylated by CKII in vitro.
    • Sequence analysis revealed homology to herpesvirus proteins and identified consensus CKII sites.
    • Mutagenesis of the CKII site significantly reduced in vitro SM phosphorylation by CKII.
    • SM transactivates gene expression by increasing cytoplasmic mRNA, independent of its CKII phosphorylation site.

    Conclusions:

    • The EBV SM protein is a highly abundant phosphoprotein crucial for early viral replication.
    • Phosphorylation of SM by CKII is demonstrated, with a key site identified and mutated.
    • SM protein functions as a transactivator of gene expression, enhancing mRNA levels.
    • The transactivation function of SM is independent of its casein kinase II phosphorylation site.