The nucleoprotein of severe fever with thrombocytopenia syndrome virus processes a stable hexameric ring to facilitate RNA encapsidation
Protein & Cell
; (12): 445-455, 2013.
Article
en En
| WPRIM
| ID: wpr-757792
Biblioteca responsable:
WPRO
ABSTRACT
Severe fever with thrombocytopenia syndrome virus (SFTSV), a member of the Phlebovirus genus from the Bunyaviridae family endemic to China, is the causative agent of life-threatening severe fever with thrombocytopenia syndrome (SFTS), which features high fever and hemorrhage. Similar to other negative-sense RNA viruses, SFTSV encodes a nucleocapsid protein (NP) that is essential for viral replication. NP facilitates viral RNA encapsidation and is responsible for the formation of ribonucleoprotein complex. However, recent studies have indicated that NP from Phlebovirus members behaves in inhomogeneous oligomerization states. In the present study, we report the crystal structure of SFTSV NP at 2.8 Å resolution and demonstrate the mechanism by which it processes a ringshaped hexameric form to accomplish RNA encapsidation. Key residues essential for oligomerization are identified through mutational analysis and identified to have a significant impact on RNA binding, which suggests that correct formation of highly ordered oligomers is a critical step in RNA encapsidation. The findings of this work provide new insights into the discovery of new antiviral reagents for Phlebovirus infection.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Unión Proteica
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Sitios de Unión
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Proteínas Recombinantes
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ARN Viral
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Química
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Phlebovirus
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Cristalografía por Rayos X
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Proteínas de la Nucleocápside
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Estructura Cuaternaria de Proteína
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Multimerización de Proteína
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Protein & Cell
Año:
2013
Tipo del documento:
Article