Publication

Article Metrics

Citations


Online attention

The crystal structure of the Hazara virus nucleocapsid protein

DOI: 10.1186/s12900-015-0051-3 DOI Help
PMID: 26715309 PMID Help

Authors: Rebecca Surtees (University of Leeds) , Antonio Ariza (University of Leeds) , Emma K. Punch (University of Leeds) , Chi H. Trinh (University of Leeds) , Stuart D. Dowall (University of Leeds) , Roger Hewson (University of Leeds) , Julian A. Hiscox (University of Leeds) , John N. Barr (University of Leeds) , Thomas A. Edwards (University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: BMC Structural Biology , VOL 15

State: Published (Approved)
Published: December 2015
Diamond Proposal Number(s): 8367

Open Access Open Access

Abstract: Hazara virus (HAZV) is a member of the Bunyaviridae family of segmented negative stranded RNA viruses, and shares the same serogroup as Crimean-Congo haemorrhagic fever virus (CCHFV). CCHFV is responsible for fatal human disease with a mortality rate approaching 30 %, which has an increased recent incidence within southern Europe. There are no preventative or therapeutic treatments for CCHFV-mediated disease, and thus CCHFVis classified as a hazard group 4 pathogen. In contrast HAZV is not associated with serious human disease, although infection of interferon receptor knockout mice with either CCHFV or HAZV results in similar disease progression. To characterise further similarities between HAZV and CCHFV, and support the use of HAZV as a model for CCHFV infection, we investigated the structure of the HAZV nucleocapsid protein (N) and compared it to CCHFV N. N performs an essential role in the viral life cycle by encapsidating the viral RNA genome, and thus, N represents a potential therapeutic target.

Journal Keywords: Hazara; CCHFV; Nairovirus; Nucleocapsid protein; RNP

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I02-Macromolecular Crystallography