ジャーナル: J Virol / 年: 2010 タイトル: The T=1 capsid protein of Penicillium chrysogenum virus is formed by a repeated helix-rich core indicative of gene duplication. 著者: Daniel Luque / José M González / Damiá Garriga / Said A Ghabrial / Wendy M Havens / Benes Trus / Nuria Verdaguer / José L Carrascosa / José R Castón / 要旨: Penicillium chrysogenum virus (PcV), a member of the Chrysoviridae family, is a double-stranded RNA (dsRNA) fungal virus with a multipartite genome, with each RNA molecule encapsidated in a separate ...Penicillium chrysogenum virus (PcV), a member of the Chrysoviridae family, is a double-stranded RNA (dsRNA) fungal virus with a multipartite genome, with each RNA molecule encapsidated in a separate particle. Chrysoviruses lack an extracellular route and are transmitted during sporogenesis and cell fusion. The PcV capsid, based on a T=1 lattice containing 60 subunits of the 982-amino-acid capsid protein, remains structurally undisturbed throughout the viral cycle, participates in genome metabolism, and isolates the virus genome from host defense mechanisms. Using three-dimensional cryoelectron microscopy, we determined the structure of the PcV virion at 8.0 A resolution. The capsid protein has a high content of rod-like densities characteristic of alpha-helices, forming a repeated alpha-helical core indicative of gene duplication. Whereas the PcV capsid protein has two motifs with the same fold, most dsRNA virus capsid subunits consist of dimers of a single protein with similar folds. The spatial arrangement of the alpha-helical core resembles that found in the capsid protein of the L-A virus, a fungal totivirus with an undivided genome, suggesting a conserved basic fold. The encapsidated genome is organized in concentric shells; whereas the inner dsRNA shells are well defined, the outermost layer is dense due to numerous interactions with the inner capsid surface, specifically, six interacting areas per monomer. The outermost genome layer is arranged in an icosahedral cage, sufficiently well ordered to allow for modeling of an A-form dsRNA. The genome ordering might constitute a framework for dsRNA transcription at the capsid interior and/or have a structural role for capsid stability.
全体 : Penicillium chrysogenum virus (PcV) full particles
全体
名称: Penicillium chrysogenum virus (PcV) full particles
要素
試料: Penicillium chrysogenum virus (PcV) full particles
ウイルス: Penicillium chrysogenum virus (ウイルス)
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超分子 #1000: Penicillium chrysogenum virus (PcV) full particles
超分子
名称: Penicillium chrysogenum virus (PcV) full particles / タイプ: sample / ID: 1000 / Number unique components: 1
分子量
理論値: 6.5 MDa
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超分子 #1: Penicillium chrysogenum virus
超分子
名称: Penicillium chrysogenum virus / タイプ: virus / ID: 1 / Name.synonym: PcV / NCBI-ID: 158372 / 生物種: Penicillium chrysogenum virus / 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 / Syn species name: PcV
宿主
生物種: Penicillium chrysogenum (菌類) / 別称: FUNGI
ウイルス殻
Shell ID: 1 / 名称: CP / 直径: 400 Å / T番号(三角分割数): 1
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実験情報
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構造解析
手法
ネガティブ染色法, クライオ電子顕微鏡法
解析
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: 7.8 / 詳細: 50 mM Tris-HCl pH 7.8, 5 mM EDTA,150 mM NaCl
染色
タイプ: NEGATIVE 詳細: Samples of empty- and full-enriched particles fractions were applied to one side of a holey carbon grid, blotted and plunged into liquid ethane