5OOO

Structure of the Rift Valley fever virus NSs protein core domain

5OOO の概要

• エントリーDOI: 10.2210/pdb5ooo/pdb
• 分子名称: Non-structural protein NS-S (2 entities in total)
• 機能のキーワード: non-structural protein, interferon antagonist, virulence factor, viral protein
• 由来する生物種: Rift valley fever virus (RVFV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38098.50

構造登録者

Barski, M.S.,Potter, J.A.,Schwarz-Linek, U. (登録日: 2017-08-08, 公開日: 2017-08-16, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)