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.Abstract
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 |
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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 |
UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology |
Depositing User: | Pure Connector |
Date Deposited: | 17 Nov 2014 12:58 |
Last Modified: | 08 Mar 2024 00:50 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/50981 |
DOI: | 10.1128/JVI.00223-13 |
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