Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. - Réplication des virus à ARN négatif
Journal Articles Science Year : 2015

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.
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Dates and versions

hal-01162615 , version 1 (24-11-2020)

Identifiers

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

Cite

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, 2015, 348 (6235), pp.704-7. ⟨hal-01162615⟩
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