Transcapsidation and the conserved interactions of two major structural proteins of a pair of phytoreoviruses confirm the mechanism of assembly of the outer capsid layer

Naoyuki Miyazaki, Kyoji Hagiwara, Hisashi Naitow, Takahiko Higashi, R. Holland Cheng, Tomitake Tsukihara, Atsushi Nakagawa, Toshihiro Omura

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

The strongly conserved amino acid sequences of the P8 outer capsid proteins of Rice dwarf virus (RDV) and Rice gall dwarf virus (RGDV) and the distribution of electrostatic potential on the proteins at the interfaces between structural proteins suggested the possibility that P8-trimers of RGDV might bind to the 3-fold symmetrical axes of RDV core particles, with vertical interaction between heterologous P3 and P8 proteins and lateral binding of homologous P8 proteins, thereby allowing formation of the double-layered capsids that are characteristic of viruses that belong to the family Reoviridae. We proved this hypothesis using chimeric virus-like particles composed of the P3 core capsid protein of RDV and the P8 outer capsid protein of RGDV, which were co-expressed in a baculovirus expression system. This is the first report on the molecular biological proof of the mechanism of the assembly of the double-layered capsids with disparate icosahedral lattices.

Original languageEnglish (US)
Pages (from-to)229-237
Number of pages9
JournalJournal of Molecular Biology
Volume345
Issue number2
DOIs
StatePublished - Jan 14 2005
Externally publishedYes

Keywords

  • baculovirus expression
  • Phytoreovirus
  • Rice dwarf virus
  • Rice gall dwarf virus
  • self-assembly

ASJC Scopus subject areas

  • Virology

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