Interactions of the borna disease virus P, N, and X proteins and their functional implications. Academic Article uri icon

Overview

abstract

  • Borna disease virus (BDV) causes persistent central nervous system infection and behavioral disturbances in warm-blooded animals. Protein interaction studies were pursued to gain insight into the functions of the putative nucleoprotein (N), phosphoprotein (P), atypical glycoprotein (gp18), and X protein (X) of BDV. Coimmunoprecipitation experiments indicated that N and P, and P and X, form complexes in infected cells. Two-hybrid analyses confirmed interactions between P and P, P and X, and P and N, but not between P and gp18, N and gp18, X and gp18, or X and N. Analysis of P truncation mutants identified three nonoverlapping regions important for oligomerization (amino acids (aa) 135-172), and binding to X (aa 33-115) or N (aa 197-201). Coexpression of X stimulated oligomerization of P but decreased N-P complex formation. Immunocytochemistry of transfected noninfected CHO cells demonstrated that the distribution of X is dependent upon the presence of P-X expressed alone was found predominantly in the cytoplasm whereas coexpression of X and P resulted in nuclear localization. Immunocytochemistry of infected cells revealed nuclear colocalization of P and X. Interactions of P, N, and X may have implications for regulation of BDV transcription/replication and ribonucleoprotein assembly.

publication date

  • April 10, 1998

Research

keywords

  • Borna disease virus
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Viral Proteins

Identity

Scopus Document Identifier

  • 0032502725

Digital Object Identifier (DOI)

  • 10.1074/jbc.273.15.9007

PubMed ID

  • 9535888

Additional Document Info

volume

  • 273

issue

  • 15