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Herpes simplex virus interferes with amyloid precursor protein processing.

Suzanne J Shipley1, Edward T Parkin, Ruth F Itzhaki

  • 1Faculty of Life Sciences, University of Manchester, Manchester, M60 1QD, UK. s.shipley@postgrad.manchester.ac.uk

BMC Microbiology
|August 20, 2005
PubMed
Summary
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Herpes simplex virus (HSV) infection rapidly alters amyloid precursor protein (APP) processing in human neuronal cells. This suggests a direct link between viral infection and Alzheimer's disease (AD) pathology.

Area of Science:

  • Neuroscience
  • Virology
  • Molecular Biology

Background:

  • Alzheimer's disease (AD) etiology is uncertain, but environmental factors like herpes simplex virus type 1 (HSV1) and APOE-epsilon4 carriage are implicated.
  • AD involves abnormal aggregation of beta-amyloid (Abeta), derived from amyloid precursor protein (APP).
  • HSV1's direct impact on APP metabolism in human neuronal cells was previously uninvestigated.

Purpose of the Study:

  • To investigate the effects of acute herpesvirus infection on amyloid precursor protein (APP) metabolism and degradation in human neuronal-type cells.
  • To determine if HSV1 directly influences APP processing.

Main Methods:

  • Human neuroblastoma cells (normal and APP 695 transfected) were infected with HSV1.
  • Western blotting was used to examine APP levels and fragments post-infection.

Related Experiment Videos

Main Results:

  • Acute HSV1 and HSV2 infection rapidly decreased full-length APP levels.
  • A novel 55 kDa C-terminal APP fragment showed a marked increase following infection.
  • This fragment increase was independent of new protein synthesis, as shown by cycloheximide treatment.

Conclusions:

  • Herpesvirus infection causes a rapid reduction in full-length APP and increases a novel 55 kDa C-terminal APP fragment.
  • These findings indicate that herpesvirus infection can directly alter APP processing.
  • Altered APP processing by herpesvirus may contribute to the development of Alzheimer's disease.