Recombinant hepatitis E capsid protein self-assembles into a dual-domain T = 1 particle presenting native virus epitopes

Li Xing, Kenzo Kato, Tiancheng Li, Naokazu Takeda, Tatsuo Miyamura, Lena Hammar, R. Holland Cheng

Research output: Contribution to journalArticle

100 Scopus citations

Abstract

The three-dimensional structure of a self-assembled, recombinant hepatitis E virus particle has been solved to 22-Å resolution by cryo- electron microscopy and three-dimensional image reconstruction. The single subunit of 50 kDa is derived from a truncated version of the open reading frame-2 gene of the virus expressed in a baculovirus system. This is the first structure of a T = 1 particle with protruding dimers at the icosahedral two-fold axes solved by cryo-electron microscopy. The protein shell of these hollow particles extends from a radius of 50 Å outward to a radius of 135 Å. In the reconstruction, the capsid is dominated by dimers that define the 30 morphological units. The outer domain of the homodimer forms a protrusion, which corresponds to the spike-like density seen in the cryo-electron micrograph. This particle retains native virus epitopes, suggesting its potential value as a vaccine.

Original languageEnglish (US)
Pages (from-to)35-45
Number of pages11
JournalVirology
Volume265
Issue number1
DOIs
StatePublished - Dec 5 1999
Externally publishedYes

Keywords

  • Cryo-EM image reconstruction
  • Human hepatitis E virus
  • Quasi- equivalence
  • Recombinant virus-like particle

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases

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