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Rinderpest virus C and V proteins interact with the major (L) component of the viral polymerase

D A Sweetman1, J Miskin, M D Baron

  • 1Institute for Animal Health, Ash Road, Surrey, Pirbright, GU24 0NF, United Kingdom.

Virology
|March 30, 2001
PubMed

Insights

Rinderpest virus C and V proteins, though not essential, aid viral replication. The V protein interacts with nucleocapsid (N) and polymerase (L) proteins, while C protein binds L and self-associates.

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Interactions

Background:

  • Rinderpest virus, a Morbillivirus, encodes P, V, and C proteins from a single P gene.
  • The functions of V and C proteins in the viral life cycle are not fully understood.
  • While dispensable for viability, C and V proteins appear to optimize viral replication.

Purpose of the Study:

  • To investigate the interactions of rinderpest virus C and V proteins with other viral proteins.
  • To elucidate the roles of C and V proteins in the viral life cycle.

Main Methods:

  • Yeast-two hybrid system to detect protein-protein interactions.
  • Glutathione-S-transferase (GST) pull-down assays.
  • Analysis of native protein size to study self-association.

Main Results:

  • Rinderpest virus V protein interacts with both nucleocapsid (N) and polymerase (L) proteins.
  • Rinderpest virus C protein binds to the L protein.
  • C protein was observed to self-associate into high-molecular-weight aggregates.

Conclusions:

  • The V protein interacts with key components of the viral replication machinery (N and L proteins).
  • The C protein interacts with the L protein and exhibits self-association.
  • These interactions likely contribute to the optimized viral replication observed when C and V proteins are expressed.

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