In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein

J Gen Virol. 1994 Nov;75 ( Pt 11):2889-96. doi: 10.1099/0022-1317-75-11-2889.

Abstract

The rabies virus phosphoprotein (P) and nucleoprotein (N) are involved in transcription and replication of the viral genome. Interaction between N and P was studied in vivo in transfected cells expressing both proteins. Co-immunoprecipitation assays revealed that the N-P complex is present in cells expressing both proteins as well as in infected cells. Furthermore, immunostaining showed that coexpression of N and P was sufficient to induce the formation of cytoplasmic inclusions similar to those found in infected cells. In addition, deletion mutant analysis of P was performed to identify the regions of P interacting with N. The results indicate that at least two independent N-binding sites exist on P protein: one is located in the carboxy-terminal part of the protein and another between amino acids 69 and 177. The formation of cytoplasmic inclusions seems to require the presence of both N-binding sites on P protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Line
  • Cricetinae
  • DNA Primers
  • Gene Deletion
  • Genes, Viral
  • Immunoblotting
  • Kidney
  • Molecular Sequence Data
  • Nucleoproteins / biosynthesis
  • Nucleoproteins / isolation & purification
  • Nucleoproteins / metabolism*
  • Phosphoproteins / biosynthesis
  • Phosphoproteins / isolation & purification
  • Phosphoproteins / metabolism*
  • Polymerase Chain Reaction
  • RNA, Messenger / metabolism
  • Rabies virus / metabolism*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / metabolism
  • Transfection
  • Viral Proteins / biosynthesis
  • Viral Proteins / isolation & purification
  • Viral Proteins / metabolism*

Substances

  • DNA Primers
  • Nucleoproteins
  • Phosphoproteins
  • RNA, Messenger
  • Recombinant Proteins
  • Viral Proteins