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J Biol Chem, Vol. 274, Issue 43, 30722-30728, October 22, 1999
From the The nonstructural protein 3 (NS3) of hepatitis C
virus (HCV) inhibits the nuclear transport and the enzymatic activity
of the catalytic subunit of protein kinase A. This inhibition is mediated by an arginine-rich domain localized between amino acids 1487-1500 of the HCV polyprotein. The data presented here indicate that the arginine-rich domain, when embedded in recombinant fragments of NS3, interacts with the catalytic site of protein kinase C (PKC) and
inhibits the phosphorylation mediated by this enzyme in
vitro and in vivo. Furthermore, a direct binding of
PKC to the NS3 fragments leads to an inhibition of the free shuttling of the kinase between the cytoplasm and the particulate fraction. In
contrast, a peptide corresponding to the arginine-rich domain (HCV
(1487-1500)), despite also being a PKC inhibitor, did not influence
the PKC shuttling process and was transported to the particulate
fraction by the translocating kinase upon activation with
tetradecanoylphorbol-13-acetate. Using the
tetradecanoylphorbol-13-acetate -stimulated respiratory burst of
NS3-introduced neutrophils as a model system, we could demonstrate that
NS3 is able to block PKC-mediated functions within intact cells. Our
data support the possibility that NS3 disrupts the PKC-mediated signal transduction.
Protein Kinase C Recognizes the Protein Kinase A-binding Motif of
Nonstructural Protein 3 of Hepatitis C Virus
,
Abteilung für Virologie,
Bernhard-Nocht-Institut für Tropenmedizin, Bernhard-Nocht-Straße
74, 20359 Hamburg, Germany and the ¶ Institut für
Medizinische Mikrobiologie und Immunologie,
Universitätskrankenhaus Eppendorf, Martinistra
e 52, 20246 Hamburg, Germany
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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