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Journal of Virology, January 2009, p. 1135-1139, Vol. 83, No. 2
0022-538X/09/$08.00+0 doi:10.1128/JVI.01808-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Université Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, BP 181, 38042 Grenoble cedex 9, France,1 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,2 Institut de Biologie Structurale Jean-Pierre Ebel, UMR5075 CEA-CNRS-Université Joseph Fourier, 41 Rue Jules Horowitz, 38027 Grenoble cedex 1, France,3 Laboratoire de Virologie Médicale, Centre de Biologie et Pathologie Est, Hospices Civils de Lyon, 59 Boulevard Pinel, F-69677 Bron, France4
Received 28 August 2008/ Accepted 17 October 2008
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 toward the facet periphery. Here we present a cryoelectron microscopy 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 than the wild-type protein, and Fabs directed against the tag bind to both ends of the oligomer, demonstrating that the pIX C termini associate in an antiparallel manner.
Published ahead of print on 12 November 2008.
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