+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-8916 | |||||||||
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タイトル | Single-particle reconstruction of reovirus T1L | |||||||||
マップデータ | Surface rendering of Reovirus T1L | |||||||||
試料 | Reovirus != Reovirus sp. Reovirus
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生物種 | Reovirus sp. (ウイルス) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 8.2 Å | |||||||||
データ登録者 | Snyder AJ / Wang JCY / Danthi P | |||||||||
引用 | ジャーナル: J Virol / 年: 2019 タイトル: Components of the Reovirus Capsid Differentially Contribute to Stability. 著者: Anthony J Snyder / Joseph Che-Yen Wang / Pranav Danthi / 要旨: The mammalian orthoreovirus (reovirus) outer capsid is composed of 200 μ1-σ3 heterohexamers and a maximum of 12 σ1 trimers. During cell entry, σ3 is degraded by luminal or intracellular proteases ...The mammalian orthoreovirus (reovirus) outer capsid is composed of 200 μ1-σ3 heterohexamers and a maximum of 12 σ1 trimers. During cell entry, σ3 is degraded by luminal or intracellular proteases to generate the infectious subviral particle (ISVP). When ISVP formation is prevented, reovirus fails to establish a productive infection, suggesting proteolytic priming is required for entry. ISVPs are then converted to ISVP*s, which is accompanied by μ1 rearrangements. The μ1 and σ3 proteins confer resistance to inactivating agents; however, neither the impact on capsid properties nor the mechanism (or basis) of inactivation is fully understood. Here, we utilized T1L/T3D M2 and T3D/T1L S4 to investigate the determinants of reovirus stability. Both reassortants encode mismatched subunits. When μ1-σ3 were derived from different strains, virions resembled wild-type particles in structure and protease sensitivity. T1L/T3D M2 and T3D/T1L S4 ISVPs were less thermostable than wild-type ISVPs. In contrast, virions were equally susceptible to heating. Virion associated μ1 adopted an ISVP*-like conformation concurrent with inactivation; σ3 preserves infectivity by preventing μ1 rearrangements. Moreover, thermostability was enhanced by a hyperstable variant of μ1. Unlike the outer capsid, the inner capsid (core) was highly resistant to elevated temperatures. The dual layered architecture allowed for differential sensitivity to inactivating agents. Nonenveloped and enveloped viruses are exposed to the environment during transmission to a new host. Protein-protein and/or protein-lipid interactions stabilize the particle and protect the viral genome. Mammalian orthoreovirus (reovirus) is composed of two concentric, protein shells. The μ1 and σ3 proteins form the outer capsid; contacts between neighboring subunits are thought to confer resistance to inactivating agents. We further investigated the determinants of reovirus stability. The outer capsid was disrupted concurrent with the loss of infectivity; virion associated μ1 rearranged into an altered conformation. Heat sensitivity was controlled by σ3; however, particle integrity was enhanced by a single μ1 mutation. In contrast, the inner capsid (core) displayed superior resistance to heating. These findings reveal structural components that differentially contribute to reovirus stability. | |||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_8916.map.gz | 193.8 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-8916-v30.xml emd-8916.xml | 7.3 KB 7.3 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_8916.png | 35 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-8916 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8916 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_8916_validation.pdf.gz | 78 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_8916_full_validation.pdf.gz | 77.1 KB | 表示 | |
XML形式データ | emd_8916_validation.xml.gz | 494 B | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8916 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8916 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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-マップ
ファイル | ダウンロード / ファイル: emd_8916.map.gz / 形式: CCP4 / 大きさ: 244.1 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Surface rendering of Reovirus T1L | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 2.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
-試料の構成要素
-全体 : Reovirus
全体 | 名称: Reovirus (ウイルス) |
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要素 |
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-超分子 #1: Reovirus sp.
超分子 | 名称: Reovirus sp. / タイプ: virus / ID: 1 / 親要素: 0 / NCBI-ID: 10891 / 生物種: Reovirus sp. / ウイルスタイプ: VIRION / ウイルス・単離状態: STRAIN / ウイルス・エンベロープ: No / ウイルス・中空状態: No |
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Host system | 生物種: Mus musculus (ハツカネズミ) |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.4 |
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凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | JEOL 3200FS |
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撮影 | フィルム・検出器のモデル: DIRECT ELECTRON DE-20 (5k x 3k) 平均電子線量: 20.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD |
-画像解析
最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 8.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 10568 |
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初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |