JVI Accepts, published online ahead of print on 12 November 2008
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J. Virol. doi:10.1128/JVI.01808-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The C-terminal domains of Adenovirus serotype 5 protein IX assemble into an anti-parallel structure on the facets of the capsid

Céline M.S Fabry, Manuel Rosa-Calatrava, Christine Moriscot, Rob W.H. Ruigrok, Pierre Boulanger, and Guy Schoehn*

Université Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, BP 181, 38042 Grenoble cedex 9, France; Université Lyon, Faculté de Médecine Laennec, Laboratoire de Virologie et Pathologie Humaine, CNRS-FRE-3011 VirPath, 7, Rue Guillaume Paradin, F-69372 Lyon Cedex 08, France; Institut de Biologie Structurale Jean-Pierre Ebel, UMR5075 CEA-CNRS-Université Joseph Fourier, 41 rue Jules Horowitz, 38027 Grenoble cedex 1, France; Laboratoire de Virologie Médicale, Centre de Biologie et Pathologie Est, Hospices Civils de Lyon, 59, Boulevard Pinel, F-69677 Bron, France

* To whom correspondence should be addressed. Email: schoehn{at}embl.fr.


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Abstract

Adenovirus serotype 5 protein IX (pIX) has two domains connected by a flexible linker. Three N-terminal domains form triskelions on the capsid facets that cement hexons together and the C-terminal domains of four monomers form complexes towards the facet periphery. Here we present a cryo-EM structure of recombinant adenovirus with a peptide tag added to the C-terminus of pIX. The structure made up by several C-termini of pIX is longer at both ends compared to wt protein and Fabs directed against the tag bind to both ends of the oligomer, demonstrating that the pIX C-termini associate in an anti-parallel manner.




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