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, Michael G. Rossmann

Research output: Contribution to journalArticle

5 Citations (Scopus)

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.

Original languageEnglish (US)
Article number388
JournalNature Communications
Volume10
Issue number1
DOIs
StatePublished - Dec 1 2019
Externally publishedYes

Fingerprint

Capsid
Capsid Proteins
viruses
Viruses
atomic structure
DNA Viruses
proteins
deoxyribonucleic acid
Tapes
DNA
Paramecium
Chlorella
tapes
Viral Structures
paramecia
Virion
Proteins
Giant Viruses
assembly

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Fang, Q., Zhu, D., Agarkova, I., Adhikari, J., Klose, T., Liu, Y., ... Rossmann, M. G. (2019). Near-atomic structure of a giant virus. Nature Communications, 10(1), [388]. https://doi.org/10.1038/s41467-019-08319-6

Near-atomic structure of a giant virus. / Fang, Qianglin; Zhu, Dongjie; Agarkova, Irina; Adhikari, Jagat; Klose, Thomas; Liu, Yue; Chen, Zhenguo; Sun, Yingyuan; Gross, Michael L.; Van Etten, James L.; Zhang, Xinzheng; Rossmann, Michael G.

In: Nature Communications, Vol. 10, No. 1, 388, 01.12.2019.

Research output: Contribution to journalArticle

Fang, Q, Zhu, D, Agarkova, I, Adhikari, J, Klose, T, Liu, Y, Chen, Z, Sun, Y, Gross, ML, Van Etten, JL, Zhang, X & Rossmann, MG 2019, 'Near-atomic structure of a giant virus', Nature Communications, vol. 10, no. 1, 388. https://doi.org/10.1038/s41467-019-08319-6
Fang Q, Zhu D, Agarkova I, Adhikari J, Klose T, Liu Y et al. Near-atomic structure of a giant virus. Nature Communications. 2019 Dec 1;10(1). 388. https://doi.org/10.1038/s41467-019-08319-6
Fang, Qianglin ; Zhu, Dongjie ; Agarkova, Irina ; Adhikari, Jagat ; Klose, Thomas ; Liu, Yue ; Chen, Zhenguo ; Sun, Yingyuan ; Gross, Michael L. ; Van Etten, James L. ; Zhang, Xinzheng ; Rossmann, Michael G. / Near-atomic structure of a giant virus. In: Nature Communications. 2019 ; Vol. 10, No. 1.
@article{75013593ec26471591d9e5ae5764613c,
title = "Near-atomic structure of a giant virus",
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 {\AA} 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.",
author = "Qianglin Fang and Dongjie Zhu and Irina Agarkova and Jagat Adhikari and Thomas Klose and Yue Liu and Zhenguo Chen and Yingyuan Sun and Gross, {Michael L.} and {Van Etten}, {James L.} and Xinzheng Zhang and Rossmann, {Michael G.}",
year = "2019",
month = "12",
day = "1",
doi = "10.1038/s41467-019-08319-6",
language = "English (US)",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

TY - JOUR

T1 - Near-atomic structure of a giant virus

AU - Fang, Qianglin

AU - Zhu, Dongjie

AU - Agarkova, Irina

AU - Adhikari, Jagat

AU - Klose, Thomas

AU - Liu, Yue

AU - Chen, Zhenguo

AU - Sun, Yingyuan

AU - Gross, Michael L.

AU - Van Etten, James L.

AU - Zhang, Xinzheng

AU - Rossmann, Michael G.

PY - 2019/12/1

Y1 - 2019/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85060381521&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85060381521&partnerID=8YFLogxK

U2 - 10.1038/s41467-019-08319-6

DO - 10.1038/s41467-019-08319-6

M3 - Article

C2 - 30674888

AN - SCOPUS:85060381521

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 388

ER -