RNA induced polymerization of the Borna disease virus nucleoprotein

Virology
Miriam HockWinfried Weissenhorn

Abstract

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.

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Citations

Aug 27, 2014·Proceedings of the National Academy of Sciences of the United States of America·Kan FujinoKeizo Tomonaga
Oct 5, 2011·Virus Research·W Ian LipkinMady Hornig
Aug 10, 2011·Current Opinion in Microbiology·Rob W H RuigrokDan Kolakofsky
Jun 21, 2013·Journal of Virology·Nicolas MartinezMarc Jamin
Dec 14, 2018·Journal of Virology·Shohei KojimaKeizo Tomonaga
Oct 8, 2021·Microbiology and Immunology·Mako YanaiKeizo Tomonaga

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