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

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Gutsche, Irina | Desfosses, Ambroise | Effantin, Grégory | Ling, Wai-Li | Haupt, Melina | Ruigrok, Rob W H | Sachse, Carsten | Schoehn, Guy

Edité par CCSD ; American Association for the Advancement of Science (AAAS) -

International audience. 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.

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