5OOO

Structure of the Rift Valley fever virus NSs protein core domain

Summary for 5OOO

• Entry DOI: 10.2210/pdb5ooo/pdb
• Descriptor: Non-structural protein NS-S (2 entities in total)
• Functional Keywords: non-structural protein, interferon antagonist, virulence factor, viral protein
• Biological source: Rift valley fever virus (RVFV)
• Total number of polymer chains: 2
• Total formula weight: 38098.50

Authors

Barski, M.S.,Potter, J.A.,Schwarz-Linek, U. (deposition date: 2017-08-08, release date: 2017-08-16, Last modification date: 2024-05-08)

Primary citation

Barski, M.,Brennan, B.,Miller, O.K.,Potter, J.A.,Vijayakrishnan, S.,Bhella, D.,Naismith, J.H.,Elliott, R.M.,Schwarz-Linek, U.
Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments.
Elife, 6:-, 2017

PubMed Abstract: Rift Valley fever phlebovirus (RVFV) is a clinically and economically important pathogen increasingly likely to cause widespread epidemics. RVFV virulence depends on the interferon antagonist non-structural protein (NSs), which remains poorly characterized. We identified a stable core domain of RVFV NSs (residues 83-248), and solved its crystal structure, a novel all-helical fold organized into highly ordered fibrils. A hallmark of RVFV pathology is NSs filament formation in infected cell nuclei. Recombinant virus encoding the NSs core domain induced intranuclear filaments, suggesting it contains all essential determinants for nuclear translocation and filament formation. Mutations of key crystal fibril interface residues in viruses encoding full-length NSs completely abrogated intranuclear filament formation in infected cells. We propose the fibrillar arrangement of the NSs core domain in crystals reveals the molecular basis of assembly of this key virulence factor in cell nuclei. Our findings have important implications for fundamental understanding of RVFV virulence.

PubMed: 28915104
DOI: 10.7554/eLife.29236

Experimental method

X-RAY DIFFRACTION (2.2 Å)