We have purified and characterized Pseudorabies virus (PRV) DNA polymerase from infected TK- mouse cells. PRV DNA polymerase has a 3'->5' exonuclease activity; it is stimulated by ionic strength, requires magnesium for optimal activity and it is more sensitive to aphidicolin than eukaryotic and HSV-1 replicative DNA polymerases. Aphidicolin inhibits in vitro PRV DNA polymerase competitively with respect to dCTP with a Ki of 0.06μM and completely blocks viral growth in vivo at 4.4μM. The high sensitivity to aphidicolin of animal herpesvirus DNA polymerases might allow a topical use of this drug in the a treatment of animal herpesvirus keratitis and stomatitis.
Aphidicolin inhibits in vitro the activity of pseudorabies virus (PRV) DNA polymerase and in vivo the viral proliferation. In vivo / A. Verri, G. Maga, S. Spadari, W. Ponti, S. Strosselli, L. Bonizzi, M. Rocchi, G. Poli, F. Focher. - In: IN VIVO. - ISSN 0258-851X. - 8:6(1994), pp. 1041-1046.
Aphidicolin inhibits in vitro the activity of pseudorabies virus (PRV) DNA polymerase and in vivo the viral proliferation. In vivo
L. Bonizzi;G. PoliPenultimo
;
1994
Abstract
We have purified and characterized Pseudorabies virus (PRV) DNA polymerase from infected TK- mouse cells. PRV DNA polymerase has a 3'->5' exonuclease activity; it is stimulated by ionic strength, requires magnesium for optimal activity and it is more sensitive to aphidicolin than eukaryotic and HSV-1 replicative DNA polymerases. Aphidicolin inhibits in vitro PRV DNA polymerase competitively with respect to dCTP with a Ki of 0.06μM and completely blocks viral growth in vivo at 4.4μM. The high sensitivity to aphidicolin of animal herpesvirus DNA polymerases might allow a topical use of this drug in the a treatment of animal herpesvirus keratitis and stomatitis.
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