2008年3月,，中科院生物物理所高光俠課題組再次于美國(guó)《國(guó)家科學(xué)院院刊》（PNAS）發(fā)表文章,，題名為：“ZAP的抗病毒功能依賴于RNA解旋酶p72”,。
宿主在與病毒長(zhǎng)期共存的過(guò)程中進(jìn)化出多種抗病毒機(jī)制,，包括表達(dá)宿主限制性因子抑制病毒的復(fù)制,。鋅指抗病毒蛋白（Zinc-finger Antiviral Protein, ZAP）是一種重要的抗病毒因子,，ZAP能通過(guò)降解特異病毒RNA進(jìn)而抑制包括鼠白血病病毒在內(nèi)的多種病毒的復(fù)制,。
文章中作者發(fā)現(xiàn),，ZAP功能的正常發(fā)揮有賴于RNA解旋酶p72。ZAP與p72之間存在不依賴RNA的直接相互作用,；過(guò)量表達(dá)p72能夠促進(jìn)ZAP的功能,；通過(guò)RNAi的方法抑制內(nèi)源表達(dá)的p72或者過(guò)量表達(dá)p72的C端,ZAP降解RNA的活性則受到抑制。進(jìn)一步研究發(fā)現(xiàn),，p72存在于ZAP與核酸外切酶復(fù)合體形成的大的復(fù)合體之中,。ZAP 抗病毒機(jī)制的研究不僅可能為病毒的防治提供新的策略和技術(shù)手段，也將有助于我們更深入了解RNA 穩(wěn)定性的調(diào)控機(jī)理。
該成果受到了國(guó)家自然科學(xué)基金,、科技部973計(jì)劃和院知識(shí)創(chuàng)新工程的資助,。（來(lái)源：中科院生物物理研究所）
生物谷推薦原始出處：
（PNAS），vol. 105 | no. 11 | 4352-4357,，Guifang Chen, Guangxia Gao
p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein
Guifang Chen, Xuemin Guo, Fengxiang Lv, Yihui Xu, and Guangxia Gao*
Center for Infections and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
Communicated by Stephen P. Goff, Columbia University, New York, NY, December 30, 2007 (received for review December 4, 2007)
The zinc-finger antiviral protein (ZAP) specifically inhibits the replication of many viruses by preventing the accumulation of viral mRNAs in the cytoplasm. ZAP directly binds to the viral mRNAs and recruits the RNA exosome to degrade the target RNA. In the present study, we identified the p72 DEAD box RNA helicase, but not the highly similar RNA helicase p68, as a ZAP-interacting protein. The binding domain of ZAP was mapped to its N-terminal portion, whereas both the N- and C-terminal domains of p72 bound to ZAP. Overexpression of the C-terminal domain of p72 reduced ZAP's activity, whereas overexpression of the full-length p72 enhanced ZAP's activity. The RNA helicase activity was required for p72 to promote ZAP-mediated RNA degradation. Depletion of p72 by RNAi also reduced ZAP's activity but did not affect tristetraprolin-mediated RNA degradation. We conclude that p72 is required for the optimal activity of ZAP, and we propose that p72 helps to restructure the ZAP-bound target mRNA for efficient degradation.
