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Borna disease virus matrix protein is an integral component of the viral ribonucleoprotein complex that does not

Geoffrey Chase1, Daniel Mayer, Antonia Hildebrand

  • 1Department of Virology, Institute for Medical Microbiology and Hygiene, University of Freiburg, Freiburg, Germany.

Journal of Virology
|November 3, 2006
PubMed

Insights

Borna disease virus matrix protein M associates with viral RNPs and phosphoprotein P. Unlike other viruses, BDV-M integrates into RNPs without inhibiting polymerase activity, aiding viral persistence.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Borna disease virus (BDV) matrix protein M was previously shown to copurify with nucleoprotein (N), suggesting RNP complex involvement.
  • Investigating M's role was limited by a lack of specific tools.

Purpose of the Study:

  • To generate an M-specific antiserum for studying BDV M protein's intracellular distribution and interactions.
  • To elucidate the role of BDV M protein in viral ribonucleoprotein complexes (RNPs) and its effect on viral polymerase activity.

Main Methods:

  • Generation of M-specific rabbit polyclonal antiserum.
  • Immunofluorescence and in situ hybridization for intracellular localization and colocalization studies.
  • Biochemical assays (minireplicon) to assess M-P binding and polymerase activity.

Main Results:

  • BDV M protein localizes to cytoplasm and nuclear punctate structures, colocalizing with nucleocapsid proteins and viral genome.
  • M specifically binds to phosphoprotein P, not N, via P's N terminus.
  • M binding to P does not inhibit, but slightly enhances, BDV polymerase activity.

Conclusions:

  • BDV M protein is an integral component of viral RNPs, directly associating with viral RNA and phosphoprotein P.
  • BDV M's unique ability to associate with RNPs without inhibiting polymerase activity is crucial for establishing viral persistence.

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