Interactions among SARS-CoV accessory proteins revealed by bimolecular fluorescence complementation assay

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• 作者：Jianqiang Kong^a ; ^{jianqiangk@imm.ac.cn" class="auth_mail" title="E-mail the corresponding author} ; Yanwei Shi^a ; Zhifang Wang^a ; Yiting Pan^b
• 关键词：aa ; amino acids ; AD ; activation domain ; BD ; binding domain ; BiFC ; bimolecular fluorescence complementation ; Co-IP ; co-immunoprecipitation ; E ; envelope ; EYFP ; enhanced yellow fluorescent protein ; M ; membrane ; N ; nucleocapsid ; NLS ; nuclear localization signal ; ORFs ; open reading frames ; PCR ; polymerase chain reaction ; PPIs ; protein-protein interactions ; PUPs ; predicted unknown proteins ; S ; spike ; SARS-CoV ; severe acute respiratory syndrome coronavirus ; Y2H ; yeast two-hybrid
• 刊名：Acta Pharmaceutica Sinica B
• 出版年：2015
• 出版时间：September 2015
• 年：2015
• 卷：5
• 期：5
• 页码：487-492
• 全文大小：2331 K

文摘

The accessory proteins (3a, 3b, 6, 7a, 7b, 8a, 8b, 9b and ORF14), predicted unknown proteins (PUPs) encoded by the genes, are considered to be unique to the severe acute respiratory syndrome coronavirus (SARS-CoV) genome. These proteins play important roles in various biological processes mediated by interactions with their partners. However, very little is known about the interactions among these accessory proteins. Here, a EYFP (enhanced yellow fluorescent protein) bimolecular fluorescence complementation (BiFC) assay was used to detect the interactions among accessory proteins. 33 out of 81 interactions were identified by BiFC, much more than that identified by the yeast two-hybrid (Y2H) system. This is the first report describing direct visualization of interactions among accessory proteins of SARS-CoV. These findings attest to the general applicability of the BiFC system for the verification of protein-protein interactions.