Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein
| Autor: | Robert M. Cox, Cynthia M. Rodenburg, Shihong Qiu, Biao He, Adrian Pickar, Jun Tsao, Terje Dokland, Ming Luo, Andrew Elson |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
viruses
Molecular Conformation RNA-dependent RNA polymerase Mumps virus Genome Viral medicine.disease_cause Virus Cell Line Transcription (biology) Cricetinae medicine Animals Nucleocapsid Polymerase Multidisciplinary biology Cryoelectron Microscopy Virion RNA RNA virus Biological Sciences biology.organism_classification Phosphoproteins RNA-Dependent RNA Polymerase Virology Molecular biology Protein Structure Tertiary Phosphoprotein biology.protein RNA Viral Plasmids Protein Binding |
| Popis: | Mumps virus (MuV) is a highly contagious pathogen, and despite extensive vaccination campaigns, outbreaks continue to occur worldwide. The virus has a negative-sense, single-stranded RNA genome that is encapsidated by the nucleocapsid protein (N) to form the nucleocapsid (NC). NC serves as the template for both transcription and replication. In this paper we solved an 18-A–resolution structure of the authentic MuV NC using cryo-electron microscopy. We also observed the effects of phosphoprotein (P) binding on the MuV NC structure. The N-terminal domain of P (PNTD) has been shown to bind NC and appeared to induce uncoiling of the helical NC. Additionally, we solved a 25-A–resolution structure of the authentic MuV NC bound with the C-terminal domain of P (PCTD). The location of the encapsidated viral genomic RNA was defined by modeling crystal structures of homologous negative strand RNA virus Ns in NC. Both the N-terminal and C-terminal domains of MuV P bind NC to participate in access to the genomic RNA by the viral RNA-dependent-RNA polymerase. These results provide critical insights on the structure-function of the MuV NC and the structural alterations that occur through its interactions with P. |
| Databáze: | OpenAIRE |
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