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Ca2+/S100 proteins regulate HCV virus NS5A–FKBP8/FKBP38 interaction and HCV virus RNA replication
https://kagawa-u.repo.nii.ac.jp/records/188
https://kagawa-u.repo.nii.ac.jp/records/1885b5fdc1c-b821-4842-a75f-354a4f855136
| 名前 / ファイル | ライセンス | アクション |
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内容の要旨 (317.8 kB)
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審査の結果の要旨 (458.8 kB)
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| Item type | 学位論文 / Thesis or Dissertation(1) | |||||||||||
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| 公開日 | 2013-06-25 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Ca2+/S100 proteins regulate HCV virus NS5A–FKBP8/FKBP38 interaction and HCV virus RNA replication | |||||||||||
| 言語 | en | |||||||||||
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| 言語 | eng | |||||||||||
| 資源タイプ | ||||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_db06 | |||||||||||
| 資源タイプ | doctoral thesis | |||||||||||
| 著者 |
谷, 丈二
× 谷, 丈二
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| 抄録 | ||||||||||||
| 内容記述タイプ | Abstract | |||||||||||
| 内容記述 | Background & Aim FKBP8/FKBP38 is a unique FK506‐binding protein with a C‐terminal membrane anchor and localizes at the outer membranes of mitochondria and the endoplasmic reticulum. Similar to some immunophilins, such as FKBP51, FKBP52 and Cyclophilin 40, FKBP8/FKBP38 contain a putative Calmodulin‐binding domain and a tetratricopeptide‐repeat (TPR) domain for the binding of Hsp90. Both Hsp90 and the non‐structural protein 5A (NS5A) of the hepatitis C virus (HCV) interact specifically with FKBP8/FKBP38 through its TPR domain, and the ternary complex formation plays a critical role in HCV RNA replication. The goal of this study is to evaluate that the host factor inhibits the ternary complex formation and the replication of HCV in vitro and in vivo. |
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| 言語 | en | |||||||||||
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| 内容記述タイプ | Abstract | |||||||||||
| 内容記述 | Methods S100 proteins, FKBP38, FKBP8, HCV NS5A, Hsp90, and calmodulin were expressed in E.coli and purified. In vitro binding studies were performed by GST pull‐down, S‐tag pull‐down and surface plasmon resonance analyses. The effect of S100 proteins on HCV replication was analysed by Western blotting using an HCV NS3 antibody following transfection of S100 proteins into the HCV replicon harbouring cell line (sO cells). |
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| 言語 | en | |||||||||||
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| 内容記述タイプ | Abstract | |||||||||||
| 内容記述 | Results In vitro binding studies showed that S100A1, S100A2, S100A6, S100B and S100P directly interacted with FKBP8/FKBP38 in a Ca2+‐dependent manner and inhibited the FKBP8/FKBP38–Hsp90 and FKBP8/FKBP38–NS5A interactions. Furthermore, overexpression of S100A1, S100A2 and S100A6 in sO cells resulted in the efficient inhibition of HCV replication. |
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| 言語 | en | |||||||||||
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| 内容記述タイプ | Abstract | |||||||||||
| 内容記述 | Conclusion The association of the S100 proteins with FKBP8/FKBP38 provides a novel Ca2+‐dependent regulatory role in HCV replication through the NS5A–host protein interaction. |
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| 言語 | en | |||||||||||
| 学位名 | ||||||||||||
| 言語 | ja | |||||||||||
| 学位名 | 博士（医学） | |||||||||||
| 学位授与機関 | ||||||||||||
| 識別子Scheme | kakenhi | |||||||||||
| 識別子 | 16201 | |||||||||||
| 言語 | ja | |||||||||||
| 機関名 | 香川大学 | |||||||||||
| 言語 | en | |||||||||||
| 機関名 | Kagawa University | |||||||||||
| 学位授与年月日 | ||||||||||||
| 学位授与年月日 | 2013-06-25 | |||||||||||
| 学位授与番号 | ||||||||||||
| 学位授与番号 | 甲第573号 | |||||||||||
| PubMed番号 | ||||||||||||
| 識別子タイプ | PMID | |||||||||||
| 関連識別子 | 23522085 | |||||||||||
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| 関連タイプ | isVersionOf | |||||||||||
| 識別子タイプ | DOI | |||||||||||
| 関連識別子 | https://doi.org/10.1111/liv.12151 | |||||||||||
| KEID | ||||||||||||
| 27456 | ||||||||||||
