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A quasi-atomic model of human adenovirus type 5 capsid
被引:113
作者:
Fabry, CMS
Rosa-Calatrava, M
Conway, JF
Zubieta, C
Cusack, S
Ruigrok, RWH
Schoehn, G
机构:
[1] Univ Grenoble 1, CNRS, FRE 2854, Lab Virol Mol & Struct, Grenoble, France
[2] Fac Med, Lab Virol & Pathogenese Virale, Lyon, France
[3] Inst Federatif Rech RTH Laennec, Lyon, France
[4] Inst Biol Struct, Grenoble, France
关键词:
cryo-electron microscopy;
minor capsid protein;
structure;
D O I:
10.1038/sj.emboj.7600653
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:1645 / 1654
页数:10
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