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

See allHide authors and affiliations

Science  08 May 2015:
Vol. 348, Issue 6235, pp. 704-707
DOI: 10.1126/science.aaa5137

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Measles virus capsid at high resolution

Viruses rely on their capsid proteins to package and protect their genome. For measles virus and other Mononegavirales family members, multiple capsid proteins together form a helical shell around the viral RNA (collectively called the nucleocapsid). Gutsche et al. now report a high-resolution cryoelectron microscopy structure of the measles virus nucleocapsid. The structure reveals how the nucleocapsid assembles and how the nucleo-protein and viral RNA interact, both of which may inform drug design

Science, this issue p. 704


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.

View Full Text

Stay Connected to Science