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Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria

M D Beatch1, T C Hobman

  • 1Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.

Journal of Virology
|May 24, 2000
PubMed

Insights

Researchers identified a host protein, p32, that interacts with the rubella virus capsid. This interaction, occurring at the mitochondria, may regulate viral nucleocapsid assembly and virus-host interactions.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Togavirus nucleocapsids exhibit icosahedral symmetry, with capsid proteins complexed with genomic RNA.
  • Rubella virus nucleocapsid assembly is unique, occurring late in viral replication and involving intracellular membranes.

Purpose of the Study:

  • To identify host cell proteins interacting with the rubella virus capsid protein.
  • To elucidate the role of host-pathogen interactions in rubella virus nucleocapsid assembly.

Main Methods:

  • Yeast two-hybrid screening of a CV1 cDNA library using rubella virus capsid as bait.
  • In vitro and in vivo validation of protein interactions.
  • Mitochondrial localization studies and observation of mitochondrial clustering upon overexpression of viral proteins.

Main Results:

  • The host protein p32 was identified as a strong interactor with the rubella virus capsid.
  • The interaction between capsid and p32 was confirmed and localized to the mitochondria.
  • Overexpression of rubella virus structural proteins induced mitochondrial clustering.
  • The p32-binding site on capsid overlaps the RNA-binding domain and is potentially phosphorylated.

Conclusions:

  • The host protein p32 interacts with the rubella virus capsid at the mitochondria.
  • This interaction may play a regulatory role in rubella virus nucleocapsid assembly.
  • The findings suggest a potential mechanism for virus-host interaction in rubella virus infection.

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