Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 26, Pages 10644-10648Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0904024106
Keywords
electron microscopy; rotavirus VP7; virus assembly; viral entry; vaccines
Categories
Funding
- National Institutes of Health [GM-62580, AI-053174, CA-13202]
- Ellison Medical Foundation New Scholars in Global Infectious Diseases
- Health Research Council of New Zealand
- Howard Hughes Medical Institute
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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 angstrom) 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 Ca2+-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.
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