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基本情報
登録情報 | データベース: EMDB / ID: EMD-23561 | |||||||||||||||||||||||||||||||||
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タイトル | CryoEM structure of T. vaginalis virus 2 capsid | |||||||||||||||||||||||||||||||||
![]() | Capsid of T. vaginalis virus 2 | |||||||||||||||||||||||||||||||||
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機能・相同性 | Capsid protein![]() | |||||||||||||||||||||||||||||||||
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手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.0 Å | |||||||||||||||||||||||||||||||||
![]() | Zhou ZH / Stevens AW / Cui YX / Muratore KA / Johnson PJ | |||||||||||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Atomic Structure of the Trichomonas vaginalis Double-Stranded RNA Virus 2. 著者: Alexander Stevens / Katherine Muratore / Yanxiang Cui / Patricia J Johnson / Z Hong Zhou / ![]() 要旨: , the causative pathogen for the most common nonviral sexually transmitted infection worldwide, is itself frequently infected with one or more of the four types of small double-stranded RNA (dsRNA) ..., the causative pathogen for the most common nonviral sexually transmitted infection worldwide, is itself frequently infected with one or more of the four types of small double-stranded RNA (dsRNA) viruses (TVV1 to 4, genus , family ). Each TVV encloses a nonsegmented genome within a single-layered capsid and replicates entirely intracellularly, like many dsRNA viruses, and unlike those in the family. Here, we have determined the structure of TVV2 by cryo-electron microscopy (cryoEM) at 3.6 Å resolution and derived an atomic model of its capsid. TVV2 has an icosahedral, T = 2*, capsid comprised of 60 copies of the icosahedral asymmetric unit (a dimer of the two capsid shell protein [CSP] conformers, CSP-A and CSP-B), typical of icosahedral dsRNA virus capsids. However, unlike the robust CSP-interlocking interactions such as the use of auxiliary "clamping" proteins among , only lateral CSP interactions are observed in TVV2, consistent with an assembly strategy optimized for TVVs' intracellular-only replication cycles within their protozoan host. The atomic model reveals both a mostly negatively charged capsid interior, which is conducive to movement of the loosely packed genome, and channels at the 5-fold vertices, which we suggest as routes of mRNA release during transcription. Structural comparison of TVV2 to the L-A virus reveals a conserved helix-rich fold within the CSP and putative guanylyltransferase domain along the capsid exterior, suggesting conserved mRNA maintenance strategies among This first atomic structure of a TVV provides a framework to guide future biochemical investigations into the interplay between and its viruses. viruses (TVVs) are double-stranded RNA (dsRNA) viruses that cohabitate in , the causative pathogen of trichomoniasis, the most common nonviral sexually transmitted disease worldwide. Featuring an unsegmented dsRNA genome encoding a single capsid shell protein (CSP), TVVs contrast with multisegmented dsRNA viruses, such as the diarrhea-causing rotavirus, whose larger genome is split into 10 dsRNA segments encoding 5 unique capsid proteins. To determine how TVVs incorporate the requisite functionalities for viral replication into their limited proteome, we derived the atomic model of TVV2, a first for TVVs. Our results reveal the intersubunit interactions driving CSP association for capsid assembly and the properties that govern organization and maintenance of the viral genome. Structural comparison between TVV2 capsids and those of distantly related dsRNA viruses indicates conserved strategies of nascent RNA release and a putative viral guanylyltransferase domain implicated in the cytoplasmic maintenance of viral messenger and genomic RNA. | |||||||||||||||||||||||||||||||||
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構造の表示
ムービー |
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構造ビューア | EMマップ: ![]() ![]() ![]() |
添付画像 |
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マップデータ | ![]() | 385.1 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 15.2 KB 15.2 KB | 表示 表示 | ![]() |
画像 | ![]() | 225.4 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 415.9 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 415.4 KB | 表示 | |
XML形式データ | ![]() | 7.6 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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リンク
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Capsid of T. vaginalis virus 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.36 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
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試料の構成要素
-全体 : Trichomonas vaginalis virus 2
全体 | 名称: ![]() |
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要素 |
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-超分子 #1: Trichomonas vaginalis virus 2
超分子 | 名称: Trichomonas vaginalis virus 2 / タイプ: virus / ID: 1 / 親要素: 0 / 含まれる分子: #1 詳細: Virus particles isolated from lysed trichomonas vaginalis NCBI-ID: 674954 / 生物種: Trichomonas vaginalis virus 2 / Sci species strain: 2 / 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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宿主 | 生物種: ![]() 株: G3 |
分子量 | 理論値: 9.40 MDa |
ウイルス殻 | Shell ID: 1 / 名称: Capsid / 直径: 430.0 Å / T番号(三角分割数): 1 |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.4 構成要素:
詳細: Sterile Solution was prepared fresh to prevent contamination. | ||||||||||||||||||
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凍結 | 凍結剤: ETHANE 詳細: The grids were manually plunged into liquid ethane.. |
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電子顕微鏡法
顕微鏡 | TFS KRIOS |
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特殊光学系 | エネルギーフィルター - 名称: GIF Quantum LS / エネルギーフィルター - スリット幅: 20 eV |
撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: SUPER-RESOLUTION / デジタル化 - サイズ - 横: 3838 pixel / デジタル化 - サイズ - 縦: 3710 pixel / 実像数: 2177 / 平均露光時間: 0.2 sec. / 平均電子線量: 17.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | C2レンズ絞り径: 50.0 µm / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 倍率(公称値): 105000 |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |