Pleomorphic Configuration of the Trimeric Capsid Proteins of Rice dwarf virus that Allows Formation of Both the Outer Capsid and Tubular Crystals

Kenji Iwasaki, Naoyuki Miyazaki, Lena Hammar, Yafeng Zhu, Toshihiro Omura, Bomu Wu, Fredrik Sjöborg, Koji Yonekura, Kazuyoshi Murata, Keiichi Namba, Donald L. Caspar, Yoshinori Fujiyoshi, R. Holland Cheng

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

In the double-shelled capsid of Phytoreovirus, the outer capsid attaches firmly to the 3-fold axes of the T = 1 core. It then forms a T = 13 lattice via lateral interactions among the P8 trimers (Wu et al., 2000, Virology 271, 18-25). Purified P8 molecules also assemble into hexagonal monolayers as well as tubular crystals. To explore the mechanisms of formation of these structures, the configurations of P8 trimers were compared and verified in particles of Rice dwarf virus and in tubular crystals (tubes) whose structure was determined by cryoelectron microscopy using helical reconstruction technique. Remarkable variations in intertrimer contacts were observed in the tubes and in the surface lattice of Rice dwarf virus capsid. Superposition of the atomic structure of P8 trimers in the structures analyzed by cryoelectron microscopy allowed us to identify groups of specific and stable interactions, some of which were preserved in the tubes and the quasi-equivalent T = 13 icosahedral lattice of the virion's shell. The flexible nature of the binding between P8 trimers, created via electrostatic interactions that hold radially inward, appears to allow the outer-capsid P8 trimers to envelop the ragged surface of the core, forming the double shell of an intact viral particle.

Original languageEnglish (US)
Pages (from-to)252-265
Number of pages14
JournalJournal of Molecular Biology
Volume383
Issue number1
DOIs
StatePublished - Oct 31 2008

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Capsid
Capsid Proteins
Viruses
Cryoelectron Microscopy
Virion
Reoviridae
Virology
Static Electricity
Oryza

Keywords

  • cryoelectron microscopy
  • Phytoreovirus
  • Rice dwarf virus

ASJC Scopus subject areas

  • Virology

Cite this

Pleomorphic Configuration of the Trimeric Capsid Proteins of Rice dwarf virus that Allows Formation of Both the Outer Capsid and Tubular Crystals. / Iwasaki, Kenji; Miyazaki, Naoyuki; Hammar, Lena; Zhu, Yafeng; Omura, Toshihiro; Wu, Bomu; Sjöborg, Fredrik; Yonekura, Koji; Murata, Kazuyoshi; Namba, Keiichi; Caspar, Donald L.; Fujiyoshi, Yoshinori; Cheng, R. Holland.

In: Journal of Molecular Biology, Vol. 383, No. 1, 31.10.2008, p. 252-265.

Research output: Contribution to journalArticle

Iwasaki, K, Miyazaki, N, Hammar, L, Zhu, Y, Omura, T, Wu, B, Sjöborg, F, Yonekura, K, Murata, K, Namba, K, Caspar, DL, Fujiyoshi, Y & Cheng, RH 2008, 'Pleomorphic Configuration of the Trimeric Capsid Proteins of Rice dwarf virus that Allows Formation of Both the Outer Capsid and Tubular Crystals', Journal of Molecular Biology, vol. 383, no. 1, pp. 252-265. https://doi.org/10.1016/j.jmb.2008.08.021
Iwasaki, Kenji ; Miyazaki, Naoyuki ; Hammar, Lena ; Zhu, Yafeng ; Omura, Toshihiro ; Wu, Bomu ; Sjöborg, Fredrik ; Yonekura, Koji ; Murata, Kazuyoshi ; Namba, Keiichi ; Caspar, Donald L. ; Fujiyoshi, Yoshinori ; Cheng, R. Holland. / Pleomorphic Configuration of the Trimeric Capsid Proteins of Rice dwarf virus that Allows Formation of Both the Outer Capsid and Tubular Crystals. In: Journal of Molecular Biology. 2008 ; Vol. 383, No. 1. pp. 252-265.
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