4.7 Article

Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid

期刊

STRUCTURE
卷 21, 期 8, 页码 1374-1383

出版社

CELL PRESS
DOI: 10.1016/j.str.2013.06.007

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资金

  1. NIAMS
  2. NIDDK
  3. IATAP grants
  4. ASCR (RVO) [61388963]
  5. US Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]

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The cystovirus phi 6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. phi 6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an alpha-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine.

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