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TitleCryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses.
Journal, issue, pagesSci Rep, Vol. 7, Issue 1, Page 5484, Year 2017
Publish dateJul 14, 2017
AuthorsChuan Xiao / Matthias G Fischer / Duer M Bolotaulo / Nancy Ulloa-Rondeau / Gustavo A Avila / Curtis A Suttle /
PubMed AbstractWhereas 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 ...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 Å and a Triangulation number of 499. Unlike related mimiviruses, the CroV capsid is not decorated with glycosylated surface fibers, but features 30 Å-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.
External linksSci Rep / PubMed:28710447 / PubMed Central
MethodsEM (single particle)
Resolution21.0 Å
Structure data

EMDB-8748:
Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests a novel assembly pathway for giant viruses
Method: EM (single particle) / Resolution: 21.0 Å

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