RNA induced polymerization of the Borna disease virus nucleoprotein.
The Borna disease virus (BDV) nucleoprotein (N) monomer resembles the nucleoprotein structures from rabies virus (RABV) and vesicular stomatitis virus (VSV). We show that BDV N assembles into ring- and string-like structures in the presence of 5' genomic BDV RNA. RNA induced polymerization is partly RNA-specific since polymerization is inefficient in the presence of 3' genomic BDV RNA or E. coli RNA. Mutagenesis of basic residues located in the cleft made up by the N- and C-terminal domains of N abrogate RNA-induced polymerization indicating that BDV N binds RNA similarly as observed in case of RABV and VSV N-RNA complexes. Bound RNA is not protected and sensitive to degradation. N-RNA polymers form complexes with the phosphoprotein P as required for functional transcription or replication units. Our data indicate that BDV N utilizes similar structural principles for N-RNA and N-P-RNA complex formation as observed for related negative strand RNA viruses.
Hock
Miriam
M
Unit of Virus Host Cell Interactions (UVHCI) UMI 3265 Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz 38042 Grenoble Cedex 9, France.
Kraus
Ina
I
Schoehn
Guy
G
Jamin
Marc
M
Andrei-Selmer
Cornelia
C
Garten
Wolfgang
W
Weissenhorn
Winfried
W
D001665:Binding Sites; D001891:Borna disease virus / Q000502:physiology*; D016297:Mutagenesis, Site-Directed; D009698:Nucleoproteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D055503:Protein Multimerization; D012367:RNA, Viral / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000378:metabolism; D014779:Virus Replication
D009698:Nucleoproteins; C496537:P protein, Borna disease virus; D010750:Phosphoproteins; D012367:RNA, Viral; D014764:Viral Proteins; D015678:Viral Structural Proteins