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Crystal Structure of the Measles Virus Nucleoprotein Core in complex with an N-terminal Region of Phosphoprotein

DOI: 10.1128/JVI.02865-15 DOI Help
PMID: 26719278 PMID Help

Authors: Sergey G. Guryanov (University of Helsinki) , Lassi Liljeroos (University of Helsinki) , Prasad Kasaragod (University of Helsinki) , Tommi Kajander (University of Helsinki) , Sarah Butcher (University of Helsinki)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Virology

State: Published (Approved)
Published: December 2015

Abstract: The enveloped negative-stranded RNA virus, measles virus (MeV) is an important human pathogen. The nucleoprotein (N0) assembles with the viral RNA into helical ribonucleocapsids (NC) which are in turn coated by a helical layer of the matrix protein. The viral polymerase complex uses the NC as its template. The N0 assembly onto the NC and the activity of the polymerase are regulated by the viral phosphoprotein (P). Here, we pulled down an N01-408 fragment lacking most of its C-terminal tail domain by several affinity-tagged, N-terminal, P fragments to map the N0-binding region of P to the first 48 amino acids. We showed biochemically and using P mutants the importance of the hydrophobic interactions for the binding. We fused an N0 binding peptide, P1-48, to the C-terminus of an N021-408 fragmentlacking both the N-terminal peptide and the C-terminal tail of N protein to reconstitute and crystallize the N0-P complex. We solved the X-ray structure of the resulting N0-P chimeric protein at 2.7 Å resolution. The structure reveals the molecular details of the conserved N0-P interface and explains how P chaperones N0 preventing both self-assembly of N0 and its binding to RNA. Finally, we propose a model for a pre-initiation complex for RNA polymerization.

Journal Keywords: Measles virus; pathogen

Subject Areas: Medicine


Instruments: I03-Macromolecular Crystallography

Added On: 28/01/2016 13:30

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