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An antiviral disulfide compound blocks interaction between arenavirus Z protein and cellular promyelocytic leukemia

C C García1, I Topisirovic, M Djavani

  • 1Laboratory of Virology, Department of Biological Chemistry, School of Sciences, University of Buenos Aires, 1428 Buenos Aires, Argentina.

Biochemical and Biophysical Research Communications
|February 16, 2010
PubMed

Insights

The compound NSC20625 prevents lymphocytic choriomeningitis virus (LCMV) from disrupting promyelocytic leukemia protein (PML) nuclear bodies (NB). This suggests NSC20625 could be a new antiviral strategy against arenavirus infections.

Area of Science:

  • Virology
  • Cell Biology
  • Drug Discovery

Background:

  • Promyelocytic leukemia protein (PML) forms nuclear bodies (NB) crucial for cellular function.
  • Virus infections, like lymphocytic choriomeningitis virus (LCMV), can disrupt PML NB.
  • The arenaviral Z protein interacts with PML, mediating this disruption.

Purpose of the Study:

  • To investigate the effect of the disulfide compound NSC20625 on the PML-Z interaction.
  • To determine if NSC20625 can restore PML NB structure disrupted by LCMV or Z protein.

Main Methods:

  • Treatment of HepG2 cells with NSC20625.
  • Infection with LCMV or transfection with Z protein constructs.
  • Analysis of PML NB distribution using microscopy.
  • Testing of Z mutants with altered zinc-binding sites.

Main Results:

  • NSC20625 treatment restored the punctate, discrete NB structure in LCMV-infected or Z-transfected cells.
  • The restoration of PML NB was observed even with a Z mutant affecting zinc-binding site 2.
  • This indicates the Z-PML interaction requires an intact zinc-binding site.

Conclusions:

  • The compound NSC20625 effectively suppresses Z-mediated disruption of PML NB.
  • NSC20625 shows potential as a therapeutic tool for novel antiviral strategies against arenavirus infections.

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