期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-017-05824-w
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资金
- Texas Advanced Computing Center from Texas [TG-MCB100154]
- NSF TeraGrid [MCB110016]
- UTEP new faculty startup fund from Texas STARs Program
- Max Planck Society
- Gottlieb Daimler-and Karl Benz-Foundation Germany
- EMBO
- University of British Columbia
- Natural Sciences and Engineering Research of Canada
- Canadian Foundation for Innovation
- British Columbia Knowledge Development Fund
Whereas the protein composition and overall shape of several giant virus capsids have been described, the mechanism by which these large capsids assemble remains enigmatic. Here, we present a reconstruction of the capsid of Cafeteria roenbergensis virus (CroV), one of the largest viruses analyzed by cryo-electron microscopy (cryo-EM) to date. The CroV capsid has a diameter of 3,000 angstrom and a Triangulation number of 499. Unlike related mimiviruses, the CroV capsid is not decorated with glycosylated surface fibers, but features 30 angstrom-long surface protrusions that are formed by loops of the major capsid protein. Based on the orientation of capsomers in the cryo-EM reconstruction, we propose that the capsids of CroV and related giant viruses are assembled by a newly conceived assembly pathway that initiates at a five-fold vertex and continuously proceeds outwards in a spiraling fashion.
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