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Science. 2015 May 8;348(6235):704-7. doi: 10.1126/science.aaa5137. Epub 2015 Apr 16.

Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid.

Author information

1
CNRS, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Université Grenoble Alpes, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. gutsche@embl.fr.
2
Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69917 Heidelberg, Germany.
3
CNRS, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Université Grenoble Alpes, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France.
4
Université Grenoble Alpes, IBS, 38044 Grenoble, France. CNRS, IBS, 38044 Grenoble, France. CEA, IBS, 38044 Grenoble, France.
5
Institut Laue-Langevin, 38000 Grenoble, France.
6
CNRS, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Université Grenoble Alpes, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Université Grenoble Alpes, IBS, 38044 Grenoble, France. CNRS, IBS, 38044 Grenoble, France. CEA, IBS, 38044 Grenoble, France.

Abstract

Measles is a highly contagious human disease. We used cryo-electron microscopy and single particle-based helical image analysis to determine the structure of the helical nucleocapsid formed by the folded domain of the measles virus nucleoprotein encapsidating an RNA at a resolution of 4.3 angstroms. The resulting pseudoatomic model of the measles virus nucleocapsid offers important insights into the mechanism of the helical polymerization of nucleocapsids of negative-strand RNA viruses, in particular via the exchange subdomains of the nucleoprotein. The structure reveals the mode of the nucleoprotein-RNA interaction and explains why each nucleoprotein of measles virus binds six nucleotides, whereas the respiratory syncytial virus nucleoprotein binds seven. It provides a rational basis for further analysis of measles virus replication and transcription, and reveals potential targets for drug design.

PMID:
25883315
DOI:
10.1126/science.aaa5137
[Indexed for MEDLINE]
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