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Nucleic Acids Research, 2003, Vol. 31, No. 16 4950-4957
© 2003 Oxford University Press

Characterisation of the substrate specificity of homogeneous vaccinia virus uracil-DNA glycosylase

Natale Scaramozzino, Guenhael Sanz1, Jean Marc Crance, Murat Saparbaev1, Robert Drillien2, Jacques Laval1, Bodil Kavli3 and Daniel Garin*

Laboratoire de Virologie, Centre de Recherches du Service de Santé des Armées (CRSSA) Emile Pardé, Grenoble, France, 1 Groupe ‘Réparation de l’ADN’, UMR 8113 CNRS, LBPA-ENS Cachan, Institut Gustave Roussy, Villejuif, France, 2 Equipe Propre INSERM 99-08, Etablissement Français du Sang-Alsace, France and 3 Institute of Cancer Research and Molecular Biology, Norwegian University of Science and Technology, N-7489 Trondheim, Norway

*To whom correspondence should be addressed at CRSSA, 24 avenue des Maquis du Grésivaudan, BP87, 38702 La Tronche cedex, France. Tel: +33 476 63 68 44; Fax: +33 476 63 69 06; Email: daniel.garin{at}wanadoo.fr
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

The decision to stop smallpox vaccination and the loss of specific immunity in a large proportion of the population could jeopardise world health due to the possibility of a natural or provoked re-emergence of smallpox. Therefore, it is mandatory to improve the current capability to prevent or treat such infections. The DNA repair protein uracil-DNA glycosylase (UNG) is one of the viral enzymes important for poxvirus pathogenesis. Consequently, the inhibition of UNG could be a rational strategy for the treatment of infections with poxviruses. In order to develop inhibitor assays for UNG, as a first step, we have characterised the recombinant vaccinia virus UNG (vUNG) and compared it with the human nuclear form (hUNG2) and catalytic fragment (hUNG) UNG. In contrast to hUNG2, vUNG is strongly inhibited in the presence of 7.5 mM MgCl2. We have shown that highly purified vUNG is not inhibited by a specific uracil-DNA glycosylase inhibitor. Interestingly, both viral and human enzymes preferentially excise uracil when it is opposite to cytosine. The present study provides the basis for the design of specific inhibitors for vUNG.


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