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p53 and proliferating cell nuclear antigen expression in JC virus-infected cells of progressive multifocal

A Ariza1, J L Mate, A Fernández-Vasalo

  • 1Department of Anatomic Pathology, Hospital Universitari Germans Trias i Pujol, Universitat Autònoma de Barcelona, Spain.

Human Pathology
|December 1, 1994
PubMed

Insights

Progressive multifocal leukoencephalopathy (PML) involves JC virus (JCV) infection, altering glial cells. Researchers found JCV T protein binding stabilizes p53, linking it to PML

Area of Science:

  • Neurovirology
  • Cellular Biology
  • Pathology

Background:

  • Progressive multifocal leukoencephalopathy (PML) is a CNS demyelinating disease caused by JC papova virus (JCV).
  • PML is characterized by atypical glial cell changes.
  • The JCV T protein interacts with the p53 tumor suppressor, potentially disrupting cell cycle regulation.

Purpose of the Study:

  • To investigate the hypothesis that JCV T protein binding stabilizes p53, prolonging its half-life and enabling immunohistochemical detection.
  • To explore the role of p53 stabilization in the pathogenesis of PML-associated glial changes.

Main Methods:

  • Combined JCV DNA in situ hybridization (ISH) and glial fibrillary acidic protein (GFAP) immunohistochemistry (IHC).
  • p53/GFAP and PCNA/GFAP double IHC on autopsy and biopsy specimens from PML patients.
  • Analysis of viral DNA, glial markers, p53, and proliferating cell nuclear antigen (PCNA) expression.

Main Results:

  • All PML specimens showed JCV-infected oligodendrocytes and atypical astrocytes with strong p53 immunostaining.
  • PCNA overexpression was observed in JCV-infected cells in biopsy specimens, indicating proliferation.
  • Evidence suggests a link between JCV-induced p53 stabilization/inactivation and tumor-like glial changes in PML.

Conclusions:

  • JCV infection leads to p53 stabilization and inactivation in glial cells.
  • This p53 alteration is implicated in the characteristic tumor-like glial changes observed in PML.
  • PCNA overexpression further supports the proposed pathogenetic mechanism involving p53 dysfunction.

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