Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway

Li Xing, Tian Cheng Li, Naoyuki Mayazaki, Martha N. Simon, Joseph S. Wall, Mary Moore, Che Yen Wang, Naokazu Takeda, Takaji Wakita, Tatsuo Miyamura, R. Holland Cheng

Research output: Contribution to journalArticle

96 Scopus citations

Abstract

Hepatitis E virus (HEV) induces acute hepatitis in humans with a high fatality rate in pregnant women. There is a need for anti-HEV research to understand the assembly process of HEV native capsid. Here, we produced a large virion-sized and a small T=1 capsid by expressing the HEV capsid protein in insect cells with and without the N-terminal 111 residues, respectively, for comparative structural analysis. The virion-sized capsid demonstrates a T=3 icosahedral lattice and contains RNA fragment in contrast to the RNA-free T=1 capsid. However, both capsids shared common decameric organization. The in vitro assembly further demonstrated that HEV capsid protein had the intrinsic ability to form decameric intermediate. Our data suggest that RNA binding is the extrinsic factor essential for the assembly of HEV native capsids.

Original languageEnglish (US)
Pages (from-to)33175-33183
Number of pages9
JournalJournal of Biological Chemistry
Volume285
Issue number43
DOIs
StatePublished - Oct 22 2010

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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    Xing, L., Li, T. C., Mayazaki, N., Simon, M. N., Wall, J. S., Moore, M., Wang, C. Y., Takeda, N., Wakita, T., Miyamura, T., & Cheng, R. H. (2010). Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway. Journal of Biological Chemistry, 285(43), 33175-33183. https://doi.org/10.1074/jbc.M110.106336