論文

査読有り
2017年2月

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

JOURNAL OF INTERFERON AND CYTOKINE RESEARCH
  • Hassan T. Tag-El-Din-Hassan
  • ,
  • Nobuya Sasaki
  • ,
  • Daisuke Torigoe
  • ,
  • Masami Morimatsu
  • ,
  • Takashi Agui

37
2
開始ページ
71
終了ページ
80
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1089/jir.2016.0012
出版者・発行元
MARY ANN LIEBERT, INC

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.

Web of Science ® 被引用回数 : 6

リンク情報
DOI
https://doi.org/10.1089/jir.2016.0012
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/27849431
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000394495900004&DestApp=WOS_CPL
ID情報
  • DOI : 10.1089/jir.2016.0012
  • ISSN : 1079-9907
  • eISSN : 1557-7465
  • PubMed ID : 27849431
  • Web of Science ID : WOS:000394495900004

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