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Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
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Nuclear body formation and PML body remodeling by the human cytomegalovirus protein UL35

Jayme Salsman1, Xueqi Wang, Lori Frappier

  • 1Department of Molecular Genetics, 1 Kings College Circle, University of Toronto, Toronto, Ontario, Canada M5S 1A8.

Virology
|April 15, 2011
PubMed

Insights

Human cytomegalovirus UL35 protein forms nuclear bodies that recruit PML proteins. UL35a protein inhibits this formation, while pp71 influences localization, impacting viral infection dynamics.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Human cytomegalovirus (HCMV) infection involves complex protein interactions.
  • The UL35 gene produces two proteins, UL35 and UL35a, with roles in viral replication.
  • Promyelocytic leukemia (PML) nuclear bodies are crucial for regulating viral gene expression.

Purpose of the Study:

  • To investigate the association between HCMV UL35 protein and PML nuclear bodies.
  • To elucidate the roles of UL35 and UL35a in nuclear body formation and localization.
  • To understand the influence of HCMV tegument protein pp71 on UL35 and UL35a.

Main Methods:

  • Cell transfection and expression of HCMV UL35 and UL35a proteins.
  • Immunofluorescence microscopy to visualize protein localization and body formation.
  • Co-immunoprecipitation assays to study protein-protein interactions.

Main Results:

  • UL35 forms nuclear bodies independently of PML, subsequently recruiting PML, Sp100, and Daxx.
  • UL35a does not form bodies but binds to UL35, inhibiting UL35 body formation.
  • HCMV pp71 promotes UL35 body formation and cytoplasmic localization of UL35a, and vice versa.

Conclusions:

  • UL35 nuclear body formation is an early event in HCMV infection, preceding PML recruitment.
  • UL35a acts as a negative regulator of UL35 body formation.
  • The interplay between UL35, UL35a, and pp71 influences viral protein localization and function during HCMV infection.

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