Near-atomic structure of a giant virus

Qianglin Fang, Dongjie Zhu, Irina Agarkova, Jagat Adhikari, Thomas Klose, Yue Liu, Zhenguo Chen, Yingyuan Sun, Michael L. Gross, James L. Van Etten, Xinzheng Zhang () and Michael G. Rossmann ()
Additional contact information
Qianglin Fang: Purdue University
Dongjie Zhu: CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Irina Agarkova: University of Nebraska-Lincoln
Jagat Adhikari: Washington University
Thomas Klose: Purdue University
Yue Liu: Purdue University
Zhenguo Chen: Purdue University
Yingyuan Sun: Purdue University
Michael L. Gross: Washington University
James L. Van Etten: University of Nebraska-Lincoln
Xinzheng Zhang: CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Michael G. Rossmann: Purdue University

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Although the nucleocytoplasmic large DNA viruses (NCLDVs) are one of the largest group of viruses that infect many eukaryotic hosts, the near-atomic resolution structures of these viruses have remained unknown. Here we describe a 3.5 Å resolution icosahedrally averaged capsid structure of Paramecium bursaria chlorella virus 1 (PBCV-1). This structure consists of 5040 copies of the major capsid protein, 60 copies of the penton protein and 1800 minor capsid proteins of which there are 13 different types. The minor capsid proteins form a hexagonal network below the outer capsid shell, stabilizing the capsid by binding neighboring capsomers together. The size of the viral capsid is determined by a tape-measure, minor capsid protein of which there are 60 copies in the virion. Homologs of the tape-measure protein and some of the other minor capsid proteins exist in other NCLDVs. Thus, a similar capsid assembly pathway might be used by other NCLDVs.

Date: 2019
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DOI: 10.1038/s41467-019-08319-6

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