Near-atomic, non-icosahedrally averaged structure of giant virus Paramecium bursaria chlorella virus 1

Qianqian Shao, Irina V. Agarkova, Eric A. Noel, David D. Dunigan, Yunshu Liu, Aohan Wang, Mingcheng Guo, Linlin Xie, Xinyue Zhao, Michael G. Rossmann, James L. Etten (), Thomas Klose () and Qianglin Fang ()
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Qianqian Shao: Sun Yat-sen University
Irina V. Agarkova: University of Nebraska-Lincoln
Eric A. Noel: University of Nebraska-Lincoln
David D. Dunigan: University of Nebraska-Lincoln
Yunshu Liu: Sun Yat-sen University
Aohan Wang: Sun Yat-sen University
Mingcheng Guo: Sun Yat-sen University
Linlin Xie: Sun Yat-sen University
Xinyue Zhao: Sun Yat-sen University
Michael G. Rossmann: Purdue University
James L. Etten: University of Nebraska-Lincoln
Thomas Klose: Purdue University
Qianglin Fang: Sun Yat-sen University

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Giant viruses are a large group of viruses that infect many eukaryotes. Although components that do not obey the overall icosahedral symmetry of their capsids have been observed and found to play critical roles in the viral life cycles, identities and high-resolution structures of these components remain unknown. Here, by determining a near-atomic-resolution, five-fold averaged structure of Paramecium bursaria chlorella virus 1, we unexpectedly found the viral capsid possesses up to five major capsid protein variants and a penton protein variant. These variants create varied capsid microenvironments for the associations of fibers, a vesicle, and previously unresolved minor capsid proteins. Our structure reveals the identities and atomic models of the capsid components that do not obey the overall icosahedral symmetry and leads to a model for how these components are assembled and initiate capsid assembly, and this model might be applicable to many other giant viruses.

Date: 2022
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DOI: 10.1038/s41467-022-34218-4

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