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Animal: RNA Viruses |
Istituto di Ricerche di Biologia Molecolare P. Angeletti (IRBM), Via Pontina Km 30.600, 00040 Pomezia (Roma), Italy1
Institut für Medizinische Mikrobiologie, Martin-Luther-Universität Halle-Wittenberg, Magdeburger Str. 6, D-06097 Halle (Saale), Germany2
Author for correspondence: Cinzia Traboni. Fax +39 06 91 09 32 25. e-mail traboni{at}irbm.it
The identification of antivirals and vaccines against hepatitis C virus (HCV) infection is hampered by the lack of convenient animal models. The need to develop surrogate models has recently drawn attention to GB virus B (GBV-B), which produces hepatitis in small primates. In a previous study in vitro, it was shown that GBV-B NS3 protease shares substrate specificity with the HCV enzyme, known to be crucial for virus replication. In this report, GBV-B NS3 activity on GBV-B precursor proteins has been analysed in a cell-based system. It is shown that mature protein products are obtained that are compatible with the cleavage sites proposed on the basis of sequence homology with HCV and that GBV-B NS4A protein is required as a cofactor for optimal enzymatic activity. Experiments in vitro supported by a structural model mapped the region of NS4A that interacts with NS3 and showed that the GBV-B cofactor cannot be substituted for by its HCV analogue.
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A. De Tomassi, M. Pizzuti, and C. Traboni Hep3B Human Hepatoma Cells Support Replication of the Wild-Type and a 5'-End Deletion Mutant GB Virus B Replicon J. Virol., November 15, 2003; 77(22): 11875 - 11881. [Abstract] [Full Text] [PDF]
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A. De Tomassi, M. Pizzuti, R. Graziani, A. Sbardellati, S. Altamura, G. Paonessa, and C. Traboni Cell Clones Selected from the Huh7 Human Hepatoma Cell Line Support Efficient Replication of a Subgenomic GB Virus B Replicon J. Virol., June 27, 2002; 76(15): 7736 - 7746. [Abstract] [Full Text] [PDF]
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