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Journal of Virology, October 2001, p. 9470-9482, Vol. 75, No. 19
Institut für Virologie (FB
Veterinärmedizin), Justus-Liebig-Universität Giessen,
D-35392 Giessen,1 and Federal
Research Center for Virus Diseases of Animals, D-72076
Tübingen,2 Germany
Received 5 April 2001/Accepted 21 June 2001
Pestiviruses are positive-strand RNA viruses closely related to
human hepatitis C virus. Gene expression of these viruses occurs via
translation of a polyprotein, which is further processed by cellular
and viral proteases. Here we report the formation of a stable complex
between an as-yet-undescribed cellular J-domain protein, a member of
the DnaJ-chaperone family, and pestiviral nonstructural protein NS2.
Accordingly, we termed the cellular protein Jiv, for J-domain protein
interacting with viral protein. Jiv has the potential to induce in
trans one specific processing step in the viral
polyprotein, namely, cleavage of NS2-3. Efficient generation of its
cleavage product NS3 has previously been shown to be obligatory for the
cytopathogenicity of the pestiviruses. Regulated expression of Jiv in
cells infected with noncytopathogenic bovine viral diarrhea virus
disclosed a direct correlation between the intracellular level of Jiv,
the extent of NS2-3 cleavage, and pestiviral cytopathogenicity.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.19.9470-9482.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
A Cellular J-Domain Protein Modulates Polyprotein
Processing and Cytopathogenicity of a Pestivirus


*
Corresponding author. Mailing address: Institut
für Virologie (FB Veterinärmedizin),
Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, D-35392 Giessen, Germany. Phone: 49 (641) 99-38375. Fax: 49 (641)
99-38359. E-mail: Norbert.Tautz{at}vetmed.uni-giessen.de.
Present address: Virco UK, Ltd., Cambridge, United Kingdom.
Present address: Chiron Corp., I-53100 Siena, Italy.
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