| Title: |
Structure of the nucleoprotein binding domain of Mokola virus phosphoprotein. |
| Authors: |
Assenberg, R; Delmas, O; Ren, J; Vidalain, P; Verma, A; Larrous, F; Graham, S; Tangy, F; Grimes, J; Bourhy, H |
| Publication Year: |
2016 |
| Collection: |
Oxford University Research Archive (ORA) |
| Description: |
Mokola virus (MOKV) is a nonsegmented, negative-sense RNA virus that belongs to the Lyssavirus genus and Rhabdoviridae family. MOKV phosphoprotein P is an essential component of the replication and transcription complex and acts as a cofactor for the viral RNA-dependent RNA polymerase. P recruits the viral polymerase to the nucleoprotein-bound viral RNA (N-RNA) via an interaction between its C-terminal domain and the N-RNA complex. Here we present a structure for this domain of MOKV P, obtained by expression of full-length P in Escherichia coli, which was subsequently truncated during crystallization. The structure has a high degree of homology with P of rabies virus, another member of Lyssavirus genus, and to a lesser degree with P of vesicular stomatitis virus (VSV), a member of the related Vesiculovirus genus. In addition, analysis of the crystal packing of this domain reveals a potential binding site for the nucleoprotein N. Using both site-directed mutagenesis and yeast two-hybrid experiments to measure P-N interaction, we have determined the relative roles of key amino acids involved in this interaction to map the region of P that binds N. This analysis also reveals a structural relationship between the N-RNA binding domain of the P proteins of the Rhabdoviridae and the Paramyxoviridae. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1128/jvi.01520-09 |
| Availability: |
https://doi.org/10.1128/jvi.01520-09; https://ora.ox.ac.uk/objects/uuid:ec143239-06d6-42a3-9004-1649c55ae004 |
| Rights: |
info:eu-repo/semantics/embargoedAccess |
| Accession Number: |
edsbas.480053D5 |
| Database: |
BASE |