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The polymerase (L) protein of rinderpest virus interacts with the host cell protein striatin

Katrina Sleeman1, Michael D Baron

  • 1Molecular Virology and Parasitology, Institute for Animal Health, Ash Road, Pirbright, Surrey GU24 0NF, UK.

Virology
|January 22, 2005
PubMed

Insights

Researchers identified striatin as a host cell protein interacting with the Rinderpest virus (RPV) L protein. This interaction, confirmed through multiple assays, primarily involves the central conserved domain of the L protein.

Area of Science:

  • Virology
  • Molecular Biology
  • Protein-protein interactions

Background:

  • Rinderpest virus (RPV) is a highly contagious morbillivirus impacting Artiodactyla.
  • The viral L protein is essential for RPV's RNA-dependent RNA polymerase activity.

Purpose of the Study:

  • To identify host cell proteins that interact with the RPV L protein.
  • To characterize the specific domain of the L protein involved in host interactions.

Main Methods:

  • Yeast two-hybrid system for library screening.
  • Co-immunoprecipitation assays to confirm protein interactions.
  • Confocal microscopy for co-localization studies.

Main Results:

  • Striatin was identified as a putative interactor of the RPV L protein.
  • Direct interaction between RPV L and striatin was confirmed experimentally.
  • Striatin co-localizes with RPV L in infected cells, primarily interacting with the L protein's central conserved domain.

Conclusions:

  • Striatin is a host cell protein that interacts with the RPV L protein.
  • The interaction between RPV L and striatin occurs within the central conserved domain of the L protein.
  • Understanding these interactions can provide insights into RPV replication and host-pathogen dynamics.

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