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 /
PubMed 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. ...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.
EMDB-5173: Cryo-EM structure of virion-sized hepatitis E virus-like particle PDB-3iyo: Cryo-EM model of virion-sized HEV virion-sized capsid Method: EM (single particle) / Resolution: 10.5 Å
Source
hepatitis e virus
Keywords
VIRUS / Amino Acid Sequence / Capsid / Capsid Proteins / Cryoelectron Microscopy / Dimerization / Image Processing / Computer-Assisted / Molecular Sequence Data / hepatitis E virus / Protein Conformation / Protein Folding / Protein Structure / Recombinant viral capsid / Virus Assembly / icosahedral virus
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