A quasi-atomic model of human adenovirus type 5 capsid

123Citations
Citations of this article
83Readers
Mendeley users who have this article in their library.

This article is free to access.

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 Å 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. © 2005 European Molecular Biology Organization | All Rights Reserved.

Cite

CITATION STYLE

APA

Fabry, C. M. S., Rosa-Calatrava, M., Conway, J. F., Zubieta, C., Cusack, S., Ruigrok, R. W. H., & Schoehn, G. (2005). A quasi-atomic model of human adenovirus type 5 capsid. EMBO Journal, 24(9), 1645–1654. https://doi.org/10.1038/sj.emboj.7600653

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free