- EMDB-3283: Cryo-EM structure of BK polyomavirus -
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基本情報
登録情報
データベース: EMDB / ID: EMD-3283
タイトル
Cryo-EM structure of BK polyomavirus
マップデータ
Reconstruction of BK polyomavirus (sharpened/masked)
試料
試料: BK polyomavirusBKウイルス
ウイルス: BK polyomavirus (BKウイルス)
キーワード
BKPyV (BKウイルス) / BK / polyomavirus (ポリオーマウイルス科)
機能・相同性
機能・相同性情報
caveolin-mediated endocytosis of virus by host cell / T=7 icosahedral viral capsid / host cell nucleus / virion attachment to host cell / structural molecule activity 類似検索 - 分子機能
Capsid protein VP1,Polyomavirus / Polyomavirus capsid protein VP1 superfamily / Polyomavirus coat protein / Double-stranded DNA virus, group I, capsid 類似検索 - ドメイン・相同性
ジャーナル: Structure / 年: 2016 タイトル: New Structural Insights into the Genome and Minor Capsid Proteins of BK Polyomavirus using Cryo-Electron Microscopy. 著者: Daniel L Hurdiss / Ethan L Morgan / Rebecca F Thompson / Emma L Prescott / Margarita M Panou / Andrew Macdonald / Neil A Ranson / 要旨: BK polyomavirus is the causative agent of several diseases in transplant patients and the immunosuppressed. In order to better understand the structure and life cycle of BK, we produced infectious ...BK polyomavirus is the causative agent of several diseases in transplant patients and the immunosuppressed. In order to better understand the structure and life cycle of BK, we produced infectious virions and VP1-only virus-like particles in cell culture, and determined their three-dimensional structures using cryo-electron microscopy (EM) and single-particle image processing. The resulting 7.6-Å resolution structure of BK and 9.1-Å resolution of the virus-like particles are the highest-resolution cryo-EM structures of any polyomavirus. These structures confirm that the architecture of the major structural protein components of these human polyomaviruses are similar to previous structures from other hosts, but give new insight into the location and role of the enigmatic minor structural proteins, VP2 and VP3. We also observe two shells of electron density, which we attribute to a structurally ordered part of the viral genome, and discrete contacts between this density and both VP1 and the minor capsid proteins.