| Literature DB >> 15861131 |
Céline M S Fabry1, Manuel Rosa-Calatrava, James F Conway, Chloé Zubieta, Stephen Cusack, Rob W H Ruigrok, Guy Schoehn.
Abstract
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 A 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.Entities:
Mesh:
Substances:
Year: 2005 PMID: 15861131 PMCID: PMC1142584 DOI: 10.1038/sj.emboj.7600653
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598