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

Authors :
Gutsche I
Desfosses A
Effantin G
Ling WL
Haupt M
Ruigrok RW
Sachse C
Schoehn G
Source :
Science (New York, N.Y.) [Science] 2015 May 08; Vol. 348 (6235), pp. 704-7. Date of Electronic Publication: 2015 Apr 16.
Publication Year :
2015

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.<br /> (Copyright © 2015, American Association for the Advancement of Science.)

Details

Language :
English
ISSN :
1095-9203
Volume :
348
Issue :
6235
Database :
MEDLINE
Journal :
Science (New York, N.Y.)
Publication Type :
Academic Journal
Accession number :
25883315
Full Text :
https://doi.org/10.1126/science.aaa5137