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Analysis of the Relationship Between Enzymatic and Antiviral Activities of the Chicken Oligoadenylate Synthetase-Like

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タイトル: Analysis of the Relationship Between Enzymatic and Antiviral Activities of the Chicken Oligoadenylate Synthetase-Like
著者: Tag-El-Din-Hassan, Hassan T. 著作を一覧する
Sasaki, Nobuya 著作を一覧する
Torigoe, Daisuke 著作を一覧する
Morimatsu, Masami 著作を一覧する
Agui, Takashi 著作を一覧する
キーワード: antiviral actions
IFNs and cytokines
infectious disease
OAS/RNase L
発行日: 2017年 2月 1日
出版者: Mary Ann Liebert
誌名: Journal of interferon & cytokine research
巻: 37
号: 2
開始ページ: 71
終了ページ: 80
出版社 DOI: 10.1089/jir.2016.0012
抄録: The oligoadenylate synthetase (OAS) is well known as an antiviral factor against the flavivirus infection in mammals. It is known that the oligoadenylate synthetase-like (ChOAS-L) gene is only present in the chicken genome. It has been shown in the previous report that the ChOAS-L possesses enzymatic activity to convert ATP into 2'-5'-linked oligoadenylates and antiviral activity against West Nile virus (WNV) replicon. Therefore, this study aimed to investigate the relationship between enzymatic and antiviral activities of ChOAS-L. Eight mutated ChOAS-L proteins were generated using either the site-directed mutagenesis or standard polymerase chain reaction protocol. The wild-type and mutated proteins were ectopically expressed in 293FT cells to analyze the enzymatic activity and in BHK-21 and BALB/3T3 cells to analyze the antiviral activity using WNV replicon. The results revealed that all mutated proteins showed no enzymatic activity except for ChOAS-L-A Delta UbL2. However, all mutated proteins showed antiviral activity to inhibit the replication of the WNV replicon except for ChOAS-L-A Delta UbL1/UbL2, which showed a partial inhibition compared to the wild-type ChOAS-L-A or other mutated proteins. These results suggest that the ChOAS-L expresses the antiflavivirus activity in a manner independent of enzymatic activity. Our results propose reconsideration of the mechanism of antiviral activity against the flavivirus replication of ChOAS-L.
Rights: Final publication is available from Mary Ann Liebert, Inc., publishers http://dx.doi.org/10.1089/jir.2016.0012
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/67605
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 安居院 高志

 

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