Chaperonin TRiC/CCT participates in replication of hepatitis C virus genome via interaction with the viral NS5B protein
To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV replication complex (RC)-rich membrane fractions prepared from cells harboring genome-length bicistronic HCV RNA at the exponential and stationar...
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| Published in | Virology (New York, N.Y.) Vol. 410; no. 1; pp. 38 - 47 |
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| Main Authors | , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
05.02.2011
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0042-6822 1096-0341 1096-0341 |
| DOI | 10.1016/j.virol.2010.10.026 |
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| Abstract | To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV replication complex (RC)-rich membrane fractions prepared from cells harboring genome-length bicistronic HCV RNA at the exponential and stationary growth phases. We found that the eukaryotic chaperonin T-complex polypeptide 1 (TCP1)-ring complex/chaperonin-containing TCP1 (TRiC/CCT) plays a role in the replication possibly through an interaction between subunit CCT5 and the viral RNA polymerase NS5B. siRNA-mediated knockdown of CCT5 suppressed RNA replication and production of the infectious virus. Gain-of-function activity was shown following co-transfection with whole eight TRiC/CCT subunits. HCV RNA synthesis was inhibited by an anti-CCT5 antibody in a cell-free assay. These suggest that recruitment of the chaperonin by the viral nonstructural proteins to the RC, which potentially facilitate folding of the RC component(s) into the mature active form, may be important for efficient replication of the HCV genome. |
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| AbstractList | To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV replication complex (RC)-rich membrane fractions prepared from cells harboring genome-length bicistronic HCV RNA at the exponential and stationary growth phases. We found that the eukaryotic chaperonin T-complex polypeptide 1 (TCP1)-ring complex/chaperonin-containing TCP1 (TRiC/CCT) plays a role in the replication possibly through an interaction between subunit CCT5 and the viral RNA polymerase NS5B. siRNA-mediated knockdown of CCT5 suppressed RNA replication and production of the infectious virus. Gain-of-function activity was shown following co-transfection with whole eight TRiC/CCT subunits. HCV RNA synthesis was inhibited by an anti-CCT5 antibody in a cell-free assay. These suggest that recruitment of the chaperonin by the viral nonstructural proteins to the RC, which potentially facilitate folding of the RC component(s) into the mature active form, may be important for efficient replication of the HCV genome.To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV replication complex (RC)-rich membrane fractions prepared from cells harboring genome-length bicistronic HCV RNA at the exponential and stationary growth phases. We found that the eukaryotic chaperonin T-complex polypeptide 1 (TCP1)-ring complex/chaperonin-containing TCP1 (TRiC/CCT) plays a role in the replication possibly through an interaction between subunit CCT5 and the viral RNA polymerase NS5B. siRNA-mediated knockdown of CCT5 suppressed RNA replication and production of the infectious virus. Gain-of-function activity was shown following co-transfection with whole eight TRiC/CCT subunits. HCV RNA synthesis was inhibited by an anti-CCT5 antibody in a cell-free assay. These suggest that recruitment of the chaperonin by the viral nonstructural proteins to the RC, which potentially facilitate folding of the RC component(s) into the mature active form, may be important for efficient replication of the HCV genome. To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV replication complex (RC)-rich membrane fractions prepared from cells harboring genome-length bicistronic HCV RNA at the exponential and stationary growth phases. We found that the eukaryotic chaperonin T-complex polypeptide 1 (TCP1)-ring complex/chaperonin-containing TCP1 (TRiC/CCT) plays a role in the replication possibly through an interaction between subunit CCT5 and the viral RNA polymerase NS5B. siRNA-mediated knockdown of CCT5 suppressed RNA replication and production of the infectious virus. Gain-of-function activity was shown following co-transfection with whole eight TRiC/CCT subunits. HCV RNA synthesis was inhibited by an anti-CCT5 antibody in a cell-free assay. These suggest that recruitment of the chaperonin by the viral nonstructural proteins to the RC, which potentially facilitate folding of the RC component(s) into the mature active form, may be important for efficient replication of the HCV genome. Abstract To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV replication complex (RC)-rich membrane fractions prepared from cells harboring genome-length bicistronic HCV RNA at the exponential and stationary growth phases. We found that the eukaryotic chaperonin T-complex polypeptide 1 (TCP1)-ring complex/chaperonin-containing TCP1 (TRiC/CCT) plays a role in the replication possibly through an interaction between subunit CCT5 and the viral RNA polymerase NS5B. siRNA-mediated knockdown of CCT5 suppressed RNA replication and production of the infectious virus. Gain-of-function activity was shown following co-transfection with whole eight TRiC/CCT subunits. HCV RNA synthesis was inhibited by an anti-CCT5 antibody in a cell-free assay. These suggest that recruitment of the chaperonin by the viral nonstructural proteins to the RC, which potentially facilitate folding of the RC component(s) into the mature active form, may be important for efficient replication of the HCV genome. |
| Author | Shoji, Ikuo Wakita, Takaji Inoue, Yasushi Suzuki, Tetsuro Hara, Hiromichi Matsuda, Mami Aizaki, Hideki Homma, Sakae Miyamura, Tatsuo Masaki, Takahiro Ando, Tomomi Shimoji, Tetsu Murakami, Kyoko Matsuura, Yoshiharu |
| Author_xml | – sequence: 1 givenname: Yasushi surname: Inoue fullname: Inoue, Yasushi organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 2 givenname: Hideki surname: Aizaki fullname: Aizaki, Hideki organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 3 givenname: Hiromichi surname: Hara fullname: Hara, Hiromichi organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 4 givenname: Mami surname: Matsuda fullname: Matsuda, Mami organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 5 givenname: Tomomi surname: Ando fullname: Ando, Tomomi organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 6 givenname: Tetsu surname: Shimoji fullname: Shimoji, Tetsu organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 7 givenname: Kyoko surname: Murakami fullname: Murakami, Kyoko organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 8 givenname: Takahiro surname: Masaki fullname: Masaki, Takahiro organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 9 givenname: Ikuo surname: Shoji fullname: Shoji, Ikuo organization: Division of Microbiology, Kobe University Graduate School of Medicine, Hyogo 650-0017, Japan – sequence: 10 givenname: Sakae surname: Homma fullname: Homma, Sakae organization: Department of Respiratory Medicine, Toho University School of Medicine, Tokyo 143-8541, Japan – sequence: 11 givenname: Yoshiharu surname: Matsuura fullname: Matsuura, Yoshiharu organization: Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 12 givenname: Tatsuo surname: Miyamura fullname: Miyamura, Tatsuo organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 13 givenname: Takaji surname: Wakita fullname: Wakita, Takaji organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 14 givenname: Tetsuro surname: Suzuki fullname: Suzuki, Tetsuro email: tesuzuki@hama-med.ac.jp organization: Department of Virology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21093005$$D View this record in MEDLINE/PubMed |
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| Snippet | To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of HCV... Abstract To identify the host factors implicated in the regulation of hepatitis C virus (HCV) genome replication, we performed comparative proteome analyses of... |
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| SubjectTerms | antibodies Cell Line, Tumor Chaperonin Chaperonins - metabolism DNA-directed RNA polymerase Gene Expression Regulation, Viral - physiology genome Hepacivirus - genetics Hepacivirus - physiology Hepatitis C virus Hepatocytes - virology Humans Infectious Disease Non-structural protein polypeptides proteome Replication RNA RNA, Viral - genetics RNA, Viral - metabolism Viral Core Proteins - genetics Viral Core Proteins - metabolism viral nonstructural proteins Viral Nonstructural Proteins - genetics Viral Nonstructural Proteins - metabolism Virus Replication - physiology viruses |
| Title | Chaperonin TRiC/CCT participates in replication of hepatitis C virus genome via interaction with the viral NS5B protein |
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