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Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses

MPG-Autoren
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Fischer,  Matthias
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://www.nature.com/articles/s41598-017-05824-w.pdf
(beliebiger Volltext)

https://doi.org/10.1038/s41598-017-05824-w
(beliebiger Volltext)

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Zitation

Xiao, C., Fischer, M., Bolotaulo, D. M., Ulloa-Rondeau, N., Avila, G. A., & Suttle, C. A. (2017). Cryo-EM reconstruction of the Cafeteria roenbergensis virus capsid suggests novel assembly pathway for giant viruses. Scientific Reports, 7: 5484, pp. 1-7. doi:10.1038/s41598-017-05824-w.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002D-9A0A-C
Zusammenfassung
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.