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

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.
Type de document :
Article dans une revue
Science, American Association for the Advancement of Science, 2015, 348 (6235), pp.704-7
Liste complète des métadonnées

http://hal.univ-grenoble-alpes.fr/hal-01162615
Contributeur : Frank Thomas <>
Soumis le : jeudi 11 juin 2015 - 09:00:40
Dernière modification le : lundi 19 février 2018 - 14:34:03

Identifiants

  • HAL Id : hal-01162615, version 1
  • PUBMED : 25883315

Collections

Citation

Irina Gutsche, Ambroise Desfosses, Grégory Effantin, Wai-Li Ling, Melina Haupt, et al.. Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid.. Science, American Association for the Advancement of Science, 2015, 348 (6235), pp.704-7. 〈hal-01162615〉

Partager

Métriques

Consultations de la notice

221