A quasi-atomic model of human adenovirus type 5 capsid
A quasi-atomic model of human adenovirus type 5 capsid
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DOI：
10.1038/sj.emboj.7600653
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发表时间：
2005-05-04
期刊：
影响因子：
11.4
通讯作者：
Schoehn, G
中科院分区：
文献类型：
--
作者：
Fabry, CMS;Rosa-Calatrava, M;Schoehn, G
腺病毒感染范围广泛的脊椎动物，包括人类。它们的二十面体衣壳由三种主要蛋白质组成：三聚六邻体形成小平面，五元是五聚体碱基和三聚体纤维蛋白的非共价复合体，位于12个衣壳顶端。几种蛋白质(IIIa、VI、VIII和IX)稳定衣壳。通过低温电子显微镜图像分析，我们获得了人腺病毒5型的10埃分辨率图谱。该图结合五元基团和六元系的X射线结构，建立了两个主要衣壳组分排列的准原子模型，并分析了六元-六元和六元-五元相互作用。次要蛋白，特别是VIII，通过比较天然和pix缺失突变病毒粒子的CryoEM图谱来定位。次要蛋白IX和IIIa位于衣壳的外侧，而蛋白在衣壳的内面以T=2的晶格组织。将衣壳组织与已知的噬菌体PRD1的X射线结构进行了比较。
Adenoviruses infect a wide range of vertebrates including humans. Their icosahedral capsids are composed of three major proteins: the trimeric hexon forms the facets and the penton, a noncovalent complex of the pentameric penton base and trimeric fibre proteins, is located at the 12 capsid vertices. Several proteins ( IIIa, VI, VIII and IX) stabilise the capsid. We have obtained a 10 angstrom resolution map of the human adenovirus 5 by image analysis from cryo-electron micrographs (cryoEMs). This map, in combination with the X-ray structures of the penton base and hexon, was used to build a quasi-atomic model of the arrangement of the two major capsid components and to analyse the hexon-hexon and hexon-penton interactions. The secondary proteins, notably VIII, were located by comparing cryoEM maps of native and pIX deletion mutant virions. Minor proteins IX and IIIa are located on the outside of the capsid, whereas protein VIII is organised with a T = 2 lattice on the inner face of the capsid. The capsid organisation is compared with the known X-ray structure of bacteriophage PRD1.