+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-20218 | |||||||||
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タイトル | CryoEM structure of human papillomavirus 16 pseudovirus in complex human alpha-defensin 5 (HD5) | |||||||||
マップデータ | CryoEM structure of human papillomavirus 16 pseudovirus in complex with human alpha-defensin 5 (HD5) | |||||||||
試料 |
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生物種 | Homo sapiens (ヒト) / Human papillomavirus type 16 (パピローマウイルス) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.9 Å | |||||||||
データ登録者 | Gulati NM / Wiens ME / Smith JG / Stewart PL | |||||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Pathog Immun / 年: 2019 タイトル: α-Defensin HD5 Stabilizes Capsid/Core Interactions. 著者: Neetu M Gulati / Masaru Miyagi / Mayim E Wiens / Jason G Smith / Phoebe L Stewart / 要旨: BACKGROUND: (HPV) is linked to nearly all cases of cervical cancer. Despite available vaccines, a deeper understanding of the immune response to HPV is needed. Human α-defensin 5 (HD5), an innate ...BACKGROUND: (HPV) is linked to nearly all cases of cervical cancer. Despite available vaccines, a deeper understanding of the immune response to HPV is needed. Human α-defensin 5 (HD5), an innate immune effector peptide, blocks infection of multiple sero-types of HPV, including high-risk HPV16. While a common mechanism of α-defensin anti-viral activity against nonenveloped viruses such as HPV has emerged, there is limited understanding of how α-defensins bind to viral capsids to block infection. 手法: We have used cryo-electron microscopy (cryoEM), mass spectrometry (MS) crosslinking and differential lysine modification studies, and molecular dynamics (MD) simulations to probe the ...手法: We have used cryo-electron microscopy (cryoEM), mass spectrometry (MS) crosslinking and differential lysine modification studies, and molecular dynamics (MD) simulations to probe the interaction of HPV16 pseudovirions (PsVs) with HD5. RESULTS: CryoEM single particle reconstruction did not reveal HD5 density on the capsid surface. Rather, increased density was observed under the capsid shell in the presence of HD5. MS studies ...RESULTS: CryoEM single particle reconstruction did not reveal HD5 density on the capsid surface. Rather, increased density was observed under the capsid shell in the presence of HD5. MS studies indicate that HD5 binds near the L1 and L2 capsid proteins and specifically near the C-terminal region of L1. MD simulations indicate that favorable electrostatic interactions can be formed between HD5 and the L1 C-terminal tail. CONCLUSIONS: A model is presented for how HD5 affects HPV16 structure and cell entry. In this model, HD5 binds to disordered regions of L1 and L2 protruding from the icosahedrally ordered capsid. HD5 ...CONCLUSIONS: A model is presented for how HD5 affects HPV16 structure and cell entry. In this model, HD5 binds to disordered regions of L1 and L2 protruding from the icosahedrally ordered capsid. HD5 acts to cement interactions between L1 and L2 and leads to a closer association of the L2/genome core with the L1 capsid. This model provides a structural rationale for our prior observation that HD5 interferes with the separation of L1 from the L2/genome complex during cell entry. | |||||||||
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_20218.map.gz | 765.6 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-20218-v30.xml emd-20218.xml | 9 KB 9 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_20218_fsc.xml | 29.4 KB | 表示 | FSCデータファイル |
画像 | emd_20218.png | 279.8 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-20218 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20218 | HTTPS FTP |
-関連構造データ
関連構造データ | C: 同じ文献を引用 (文献) |
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類似構造データ |
-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_20218.map.gz / 形式: CCP4 / 大きさ: 824 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | CryoEM structure of human papillomavirus 16 pseudovirus in complex with human alpha-defensin 5 (HD5) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.26 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 : Complex of human papillomavirus type 16 pseudovirus with human al...
全体 | 名称: Complex of human papillomavirus type 16 pseudovirus with human alpha-defensin 5 (HD5) |
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要素 |
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-超分子 #1: Complex of human papillomavirus type 16 pseudovirus with human al...
超分子 | 名称: Complex of human papillomavirus type 16 pseudovirus with human alpha-defensin 5 (HD5) タイプ: complex / ID: 1 / 親要素: 0 |
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-超分子 #3: alpha-defensin 5 (HD5)
超分子 | 名称: alpha-defensin 5 (HD5) / タイプ: complex / ID: 3 / 親要素: 1 詳細: Synthesized linear HD5 peptide (CPC Scientific, Sunnyvale, CA) was subjected to thiol-disulfide reshuffling and purified to homogeneity by reverse-phase high-pressure liquid chromatography |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-超分子 #2: Human papillomavirus type 16
超分子 | 名称: Human papillomavirus type 16 / タイプ: virus / ID: 2 / 親要素: 1 / NCBI-ID: 333760 / 生物種: Human papillomavirus type 16 / Sci species strain: pseudovirus / ウイルスタイプ: VIRION / ウイルス・単離状態: OTHER / 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: Homo sapiens (ヒト) / 組換細胞: 293TT |
-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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グリッド | 詳細: unspecified |
凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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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 FIELDBright-field microscopy |
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: 60.0 e/Å2 |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |