| RRC ID |
39306
|
| 著者 |
Xing L, Kato K, Li T, Takeda N, Miyamura T, Hammar L, Cheng RH.
|
| タイトル |
Recombinant hepatitis E capsid protein self-assembles into a dual-domain T = 1 particle presenting native virus epitopes.
|
| ジャーナル |
Virology
|
| Abstract |
The three-dimensional structure of a self-assembled, recombinant hepatitis E virus particle has been solved to 22-A 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 A outward to a radius of 135 A. 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.
|
| 巻・号 |
265(1)
|
| ページ |
35-45
|
| 公開日 |
1999-12-5
|
| DOI |
10.1006/viro.1999.0005
|
| PII |
S0042-6822(99)90005-3
|
| PMID |
10603315
|
| MeSH |
Capsid / ultrastructure*
Cryoelectron Microscopy
Epitopes / ultrastructure
Hepatitis E virus / ultrastructure*
Image Processing, Computer-Assisted
Models, Molecular
Molecular Weight
Protein Conformation
Protein Folding
Recombinant Proteins / ultrastructure
Virion / ultrastructure
|
| IF |
2.819
|
| 引用数 |
90
|
|
WOS 分野
|
VIROLOGY
|
| リソース情報 |
| ヒト・動物細胞 |
Sf9(RCB0563) |
