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通过应用临界点干燥法展示腺病毒核心中核蛋白的逐步盘绕。

Demonstration of stepwise coiling of nucleoprotein in adenovirus core by application of critical point drying.

作者信息

Yazaki K, Kurita T, Miura K

出版信息

J Virol Methods. 1983 Mar;6(3):119-25. doi: 10.1016/0166-0934(83)90023-x.

DOI:10.1016/0166-0934(83)90023-x
PMID:6863465
Abstract

Mild destruction of a virus particle to observe the organized structure of the nucleoprotein complex in a virion was achieved by application of the critical point drying method. Adenovirus type 12 (ad12) virions have been treated by this method after the particles had been fixed with glutaraldehyde on an electron microscope grid. With 15 min prefixation, the capsids (shells) and the cores were in various stages of unfolding. The core was unfolded in the filamentous structure. The thickness of these filaments was 6.7, 13.3, +23 nm, or more. Some pictures showed that the thicker filaments consisted of super-coiling of two thinner filaments, for example two 6.7-nm filaments coiled up to give the 13.3-nm filaments. This suggests that the nucleoprotein complex of a circular double-stranded DNA and inner proteins of ad12 virus was folded in a stepwise fashion to produce the compacted form of the core.

摘要

通过应用临界点干燥法,实现了对病毒颗粒的轻度破坏,以观察病毒粒子中核蛋白复合体的组织结构。12型腺病毒(ad12)病毒粒子在用戊二醛固定在电子显微镜网格上后,已用此方法处理。经过15分钟的预固定,衣壳(外壳)和核心处于不同程度的展开阶段。核心呈丝状结构展开。这些细丝的厚度为6.7、13.3、+23纳米或更厚。一些图片显示,较粗的细丝由两条较细的细丝超螺旋组成,例如两条6.7纳米的细丝盘绕在一起形成13.3纳米的细丝。这表明,ad12病毒的环状双链DNA和内部蛋白质的核蛋白复合体以逐步折叠的方式形成了紧密的核心形式。

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