Journal
JOURNAL OF VIROLOGY
Volume 84, Issue 2, Pages 1089-1096Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01520-09
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Funding
- United Kingdom Medical Research Council
- Biotechnology and Biological Sciences Research Council
- EU [LSHG-CT-2004-511960]
- Spine2Complexes [LSGH-CT-2006-031220]
- Medical Research Council [G0701506, G1100525] Funding Source: researchfish
- MRC [G0701506] Funding Source: UKRI
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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.
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