Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation

Dong, Haohao, Li, Ping, Elliott, Richard M and Dong, Changjiang (2013) Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation. Journal of Virology, 87 (10). pp. 5593-601. ISSN 0022-538X

Full text not available from this repository. (Request a copy)


Schmallenberg virus (SBV), a newly emerged orthobunyavirus (family Bunyaviridae), has spread rapidly across Europe and has caused congenital abnormalities in the offspring of cattle, sheep, and goats. Like other orthobunyaviruses, SBV contains a tripartite negative-sense RNA genome that encodes four structural and two nonstructural proteins. The nucleoprotein (N) encapsidates the three viral genomic RNA segments and plays a crucial role in viral RNA transcription and replication. Here we report the crystal structure of the bacterially expressed SBV nucleoprotein to a 3.06-Å resolution. The protomer is composed of two domains (N-terminal and C-terminal domains) with flexible N-terminal and C-terminal arms. The N protein has a novel fold and forms a central positively charged cleft for genomic RNA binding. The nucleoprotein purified under native conditions forms a tetramer, while the nucleoprotein obtained following denaturation and refolding forms a hexamer. Our structural and functional analyses demonstrate that both N-terminal and C-terminal arms are involved in N-N interaction and oligomerization and play an essential role in viral RNA synthesis, suggesting a novel mechanism for viral RNA encapsidation and transcription.

Item Type: Article
Uncontrolled Keywords: amino acid sequence,crystallography, x-ray,models, molecular,molecular sequence data,nucleoproteins,orthobunyavirus,protein conformation,protein multimerization,rna-binding proteins,sequence alignment,virus assembly,virus replication
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
Depositing User: Pure Connector
Date Deposited: 17 Nov 2014 12:58
Last Modified: 20 Oct 2022 21:32
DOI: 10.1128/JVI.00223-13

Actions (login required)

View Item View Item