+Search query
-Structure paper
Title | Three-dimensional structure of canine adenovirus serotype 2 capsid. |
---|---|
Journal, issue, pages | J Virol, Vol. 82, Issue 7, Page 3192-3203, Year 2008 |
Publish date | Jan 23, 2008 |
Authors | Guy Schoehn / Majida El Bakkouri / Céline M S Fabry / Oliver Billet / Leandro F Estrozi / Long Le / David T Curiel / Andrey V Kajava / Rob W H Ruigrok / Eric J Kremer / |
PubMed Abstract | 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 ...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. |
External links | J Virol / PubMed:18216088 / PubMed Central |
Methods | EM (single particle) |
Resolution | 12.0 - 25.0 Å |
Structure data | EMDB-1462: EMDB-1463: |