https://scholars.lib.ntu.edu.tw/handle/123456789/452424
標題: | Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication | 作者: | Chen Y.-J. Chen Y.-H. LU-PING CHOW Tsai Y.-H. Chen P.-H. Huang C.-Y.F. Chen W.-T. Hwang L.-H. |
公開日期: | 2010 | 出版社: | American Society for Biochemistry and Molecular Biology Inc. | 卷: | 285 | 期: | 36 | 起(迄)頁: | 28183-28190 | 來源出版物: | Journal of Biological Chemistry | 摘要: | The NS5A protein of the hepatitis C virus (HCV) is an integral component of the viral replicase. It also modulates cellular signaling and perturbs host interferon responses. The multifunctional characteristics of NS5A are mostly attributed to its ability to interact with various cellular proteins. This study aimed to identify the novel cellular factors that interact with NS5A and decipher the significance of this interaction in viral replication. The NS5A-interacting proteins were purified by the tandem affinity purification (TAP) procedure from cells expressing NS5A and identified by mass spectrometry. The chaperone protein Hsp72 was identified herein. In vivo protein-protein interaction was verified by co-immunoprecipitation and an in situ proximity ligation assay. In addition to NS5A, Hsp72 was also associated with other members of the replicase complex, NS3 and NS5B, suggesting that it might be directly involved in the HCV replication complex. Hsp72 plays a positive regulatory role in HCV RNA replication by increasing levels of the replicase complex, which was attributed either to the increased stability of the viral proteins in the replicase complex or to the enhanced translational activity of the internal ribosome entry site of HCV. The fact that the host chaperone protein Hsp72 is involved in HCV RNA replication may represent a therapeutic target for controlling virus production. ? 2010 by The American Society for Biochemistry and Molecular Biology, Inc. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-77956255823&doi=10.1074%2fjbc.M110.118323&partnerID=40&md5=a5214b363bce85d592ccb299b67aa326 https://scholars.lib.ntu.edu.tw/handle/123456789/452424 |
ISSN: | 00219258 | DOI: | 10.1074/jbc.M110.118323 | SDG/關鍵字: | Mass spectrometry; Purification; RNA; Viruses; Cellular factors; Cellular proteins; Cellular signaling; Co-immunoprecipitations; HCV RNA; Heat shock protein; Hepatitis C virus; In-situ; In-vivo; Integral components; Interferon response; Internal ribosome entry site; Protein-protein interactions; Tandem affinity purification; Therapeutic targets; Viral proteins; Viral replication; Viral RNA; Proteins; heat shock protein 72; nonstructural protein 3; nonstructural protein 5B; virus RNA; heat shock cognate protein 70; heat shock protein 72; NS-5 protein, hepatitis C virus; RNA directed RNA polymerase; virus protein; article; controlled study; Hepatitis C virus; human; human cell; immunoprecipitation; internal ribosome entry site; mass spectrometry; nonhuman; priority journal; protein expression; protein function; protein processing; protein protein interaction; protein purification; protein stability; RNA replication; virus replication; biosynthesis; cell line; chemistry; enzymology; Hepacivirus; metabolism; physiology; virus replication; Hepatitis C virus; Cell Line; Hepacivirus; HSC70 Heat-Shock Proteins; HSP72 Heat-Shock Proteins; Humans; RNA Replicase; RNA, Viral; Viral Nonstructural Proteins; Virus Replication |
顯示於: | 生物化學暨分子生物學科研究所 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。