Arterivirus RNA-dependent RNA polymerase: Vital enzymatic activity remains elusive
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- 作者：Kathleen C. Lehmanna ; Alexander E. Gorbalenyaa ; b ; Eric J. Snijdera ; Clara C. Posthumaa ; c.c.posthuma@lumc.nl" class="auth_mail" title="E-mail the corresponding author
- 关键词：Equine arteritis virus ; Nidovirus ; In vitro RdRp activity ; Recombinant nsp9 ; Polymerase active site mutant ; Reverse genetics
- 刊名：Virology
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：487
- 期：Complete
- 页码：68-74
- 全文大小：1017 K
文摘
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Several recombinant RdRp preparations of Equine arteritis virus (EAV) were purified.
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No primer-dependent or de novo RdRp or terminal transferase activity was shown.
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One RdRp preparation showed products resembling those of phage T7 RNA polymerase.
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Mutation of the RdRp active site aspartates to alanine crippled the EAV viability.
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Characterizing low activity RdRp in sensitive enzymatic assays requires extra care.