| Literature DB >> 25883315 |
Irina Gutsche1, Ambroise Desfosses2, Grégory Effantin3, Wai Li Ling4, Melina Haupt5, Rob W H Ruigrok3, Carsten Sachse2, Guy Schoehn6.
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.Entities:
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Year: 2015 PMID: 25883315 DOI: 10.1126/science.aaa5137
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728