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Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid.
- 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.)
- Subjects :
- Amino Acid Sequence
Cryoelectron Microscopy
Humans
Measles virus chemistry
Molecular Sequence Data
Nucleic Acid Conformation
Nucleocapsid chemistry
Nucleocapsid Proteins
Nucleoproteins chemistry
Nucleoproteins ultrastructure
Protein Structure, Secondary
RNA, Viral chemistry
RNA, Viral ultrastructure
Viral Proteins chemistry
Viral Proteins ultrastructure
Measles virology
Measles virus ultrastructure
Nucleocapsid ultrastructure
Subjects
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