論文 - 詳細
| 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 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 12 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 3.0 |
| リソース情報 | |
| ヒト・動物細胞 | Sf9(RCB0563) |