Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM
| Autor: | Philip R. Dormitzer, Xing Zhang, Nikolaus Grigorieff, A.Richard Bellamy, Ethan C. Settembre, James Z. Chen, Stephen C. Harrison, Scott T. Aoki |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Rotavirus Cryo-electron microscopy Icosahedral symmetry viruses Trimer Biology medicine.disease_cause Crystallography X-Ray Models Biological fluids and secretions Transcription (biology) medicine Protein Structure Quaternary Antigens Viral Messenger RNA Multidisciplinary Viral Core Proteins Cryoelectron Microscopy Virion RNA virus diseases Biological Sciences Molecular biology Capsid Biophysics Commentary Calcium Capsid Proteins Protein Multimerization |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 106(26) |
| ISSN: | 1091-6490 |
| Popis: | Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 Å) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal “arms” of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca 2+ -stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding. |
| Databáze: | OpenAIRE |
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