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Journal of Virology, June 2005, p. 7911-7917, Vol. 79, No. 12
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.12.7911-7917.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Wiebke Jendrsczok,1,
Jan Martin Berke,1,3
Volker Brass,1
Hubert E. Blum,1 and
Darius Moradpour1,3*
Department of Medicine II, University of Freiburg, Hugstetter Strasse 55, D-79106 Freiburg, Germany,1 Institute for Medical Microbiology, University of Basel, Petersplatz 10, CH-4003 Basel,2 Division of Gastroenterology and Hepatology, Centre Hospitalier Universitaire Vaudois, University of Lausanne, CH-1011 Lausanne, Switzerland3
Received 20 July 2004/ Accepted 18 February 2005
Protein-protein interactions involved in formation of the membrane-associated hepatitis C virus (HCV) replication complex are poorly understood. Here, we investigated nonstructural proteins with deletions in their membrane anchor domains when expressed in the context of the entire HCV polyprotein. Interactions among cytosolic domains of HCV nonstructural proteins were found not to be sufficiently strong to rescue such mutants to the membrane. Thus, the membrane anchor domains of nonstructural proteins are essential for incorporation of these proteins into the HCV replication complex while interactions among the cytosolic domains appear to be relatively weak. This feature may provide the nonstructural proteins with a certain flexibility to perform their multiple functions during HCV replication.
R.G. and W.J. contributed equally to this work.
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