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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cryoelectron Microscopy
  • Humans
  • Measles / virology*
  • Measles virus / chemistry
  • Measles virus / ultrastructure*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Nucleocapsid / chemistry
  • Nucleocapsid / ultrastructure*
  • Nucleocapsid Proteins
  • Nucleoproteins / chemistry
  • Nucleoproteins / ultrastructure
  • Protein Structure, Secondary
  • RNA, Viral / chemistry
  • RNA, Viral / ultrastructure
  • Viral Proteins / chemistry
  • Viral Proteins / ultrastructure


  • Nucleocapsid Proteins
  • Nucleoproteins
  • RNA, Viral
  • Viral Proteins
  • nucleoprotein, Measles virus

Associated data

  • PDB/4UFT