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Journal of Virology, April 2008, p. 3192-3203, Vol. 82, No. 7
0022-538X/08/$08.00+0     doi:10.1128/JVI.02393-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Three-Dimensional Structure of Canine Adenovirus Serotype 2 Capsid{triangledown}

Guy Schoehn,1,2* Majida El Bakkouri,1 Céline M. S. Fabry,1 Oliver Billet,3,4 Leandro F. Estrozi,1 Long Le,5 David T. Curiel,5 Andrey V. Kajava,6 Rob W. H. Ruigrok,1 and Eric J. Kremer3,4*

Unit for Virus Host Cell Interaction, UMR 5233, Université Joseph Fourier, EMBL, CNRS, Grenoble, France,1 Institut de Biologie Structurale Jean-Pierre Ebel, UMR5075 CEA-CNRS-UJF, Grenoble, France,2 Institut de Génétique Moléculaire de Montpellier, CNRS 5535, Montpellier, France,3 Universités Montpellier I and II, Montpellier, France,4 Division of Human Gene Therapy, Departments of Medicine, Obstetrics and Gynecology, Pathology, and Surgery, and the Gene Therapy Center, The University of Alabama at Birmingham, Birmingham, Alabama 35294,5 Centre de Recherche de Biochimie Macromoléculaire, UMR 5237 CNRS-Universités Montpellier I and II, Montpellier, France6

Received 6 November 2007/ Accepted 28 December 2007

There are more than 100 known adenovirus (AdV) serotypes, including 50 human serotypes. Because AdV-induced disease is relatively species specific, vectors derived from nonhuman serotypes may have wider clinical potential based, in part, on the lack of ubiquitous memory immunity. Whereas a few of the human serotype capsids have been studied at the structural level, none of the nonhuman serotypes has been analyzed. The basis laid by the analysis of human AdV (hAdV) has allowed us to determine and compare the three-dimensional structure of the capsid of canine serotype 2 (CAV-2) to that of hAdV serotype 5 (hAdV-5). We show that CAV-2 capsid has a smoother structure than the human serotypes. Many of the external loops found in the hAdV-5 penton base and the hexon, against which the antibody response is directed, are shorter or absent in CAV-2. On the other hand, the CAV-2 fiber appears to be more complex, with two bends in the shaft. An interesting difference between the human and canine viruses is that the C-terminal part of protein IX is in a different position, making an antenna sticking out of the CAV-2 capsid. The comparison between the two viruses allows the identification of sites that should be easy to modify on the CAV-2 capsid for altering tissue tropism or other biological activities.

* Corresponding author. Mailing address for Guy Schoehn: Unit for Virus Host Cell Interaction, 6 rue Jules Horowitz, BP181, 38042 Grenoble, France. Phone: 33 4 7620 9423. Fax: 33 4 7620 7199. E-mail: schoehn{at}embl.fr. Mailing address for Eric J. Kremer: Institut de Génétique Moléculaire de Montpellier, CNRS 5535, 1919 Route de Mende, 34293 Montpellier, France. Phone: 33 4 6761 3672. Fax: 33 4 6704 0231. E-mail: eric.kremer{at}igmm.cnrs.fr

{triangledown} Published ahead of print on 23 January 2008.

Journal of Virology, April 2008, p. 3192-3203, Vol. 82, No. 7
0022-538X/08/$08.00+0     doi:10.1128/JVI.02393-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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