Host cell factor requirement for hepatitis C virus enzyme maturation
AUTOR(ES)
Waxman, Lloyd
FONTE
The National Academy of Sciences
RESUMO
The cellular chaperone, HSP90, is identified here as an essential factor for the activity of NS2/3 protease of hepatitis C virus. The cleavage activity of NS2/3 protease synthesized in reticulocyte lysate is ATP-dependent, as evidenced by ATP depletion experiments and inhibition with nonhydrolyzable ATP analogs. Geldanamycin and radicicol, ATP-competitive inhibitors of the chaperone HSP90, also inhibit the cleavage of in vitro-synthesized NS2/3. Furthermore, these HSP90 inhibitors prevent NS2/3 cleavage when the protease is expressed in mammalian cells. The physical association of NS2/3 with HSP90 is demonstrated by immunoprecipitation. Thus, by way of a chaperone/folding activity, an HSP90-containing complex is required for maturation of the polyprotein that encodes the enzymes essential for hepatitis C virus replication.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=61144Documentos Relacionados
- Vaccinia Virus Replication I. Requirement for the Host-Cell Nucleus
- Hepatitis B virus X protein activates transcription factor NF-kappa B without a requirement for protein kinase C.
- Efficient hepatitis C virus cell culture system: What a difference the host cell makes
- Cell-dependent requirement of human immunodeficiency virus type 1 Vif protein for maturation of virus particles.
- Assessment of commercial enzyme immunoassay for hepatitis C virus serotyping.
