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Hokkaido University Collection of Scholarly and Academic Papers >
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Analysis of the Relationship Between Enzymatic and Antiviral Activities of the Chicken Oligoadenylate Synthetase-Like
| Title: | Analysis of the Relationship Between Enzymatic and Antiviral Activities of the Chicken Oligoadenylate Synthetase-Like |
| Authors: | Tag-El-Din-Hassan, Hassan T. Browse this author | | Sasaki, Nobuya Browse this author →KAKEN DB | | Torigoe, Daisuke Browse this author | | Morimatsu, Masami Browse this author →KAKEN DB | | Agui, Takashi Browse this author →KAKEN DB |
| Keywords: | antiviral actions | | IFNs and cytokines | | infectious disease | | OAS/RNase L |
| Issue Date: | 1-Feb-2017 |
| Publisher: | Mary Ann Liebert |
| Journal Title: | Journal of interferon & cytokine research |
| Volume: | 37 |
| Issue: | 2 |
| Start Page: | 71 |
| End Page: | 80 |
| Publisher DOI: | 10.1089/jir.2016.0012 |
| PMID: | 27849431 |
| Abstract: | 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 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/67605 |
| Appears in Collections: | 獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 安居院 高志
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