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Characterization of RNase activity and translation regulation of Pseudorabies virus VHS protein
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|摘要:||假性狂犬病毒(PRV) ，隸屬疱疹病毒科之α-疱疹病毒亞科，為一具有的封套雙股線性DNA病毒，在此分類病毒中又以人類單純疱疹病毒(HSV-1)最具代表性。vhs (virion host shutoff)蛋白位於成熟病毒顆粒的殼膜區間(tegument)，由UL41 基因所轉譯，此段基因在所有α-疱疹病毒中有高度的同源性，若將PRV、HSV-1及HSV-2的vhs胺基酸序列比較可劃定四個高度保留的區域(box)。目前對於疱疹病毒vhs蛋白的研究以HSV-1為主；已知其具有RNase 活性無論是mRNA或不帶cap和poly(A)的RNA都可由五端往三端的方向性降解，但無法降解具有高度二級結構的IRES RNA序列。此外，HSV-1 vhs蛋白的RNase活性會受到細胞轉譯起始因子(eIF4 factors)的促進，並透過transcription control和posttranscription control調控宿主細胞的蛋白表現、幫助病毒的DNA複製。2004年時林等首度證實PRV vhs蛋白具有降解RNA的能力，但由於HSV-1 和PRV 之vhs 胺基酸序列相似度僅約38.4%，兩者的vhs 生物特性可能不盡相同，因此本研究將對於PRV vhs蛋白的RNA降解特性，和對細胞內的轉譯調控機制等做進一步探討。
實驗的方向可分為探討PRV vhs蛋白核酸分解活性的in vitro assay和觀察PRV vhs對細胞蛋白表現影響的in vivo assay兩部份。在in vitro的實驗中，再次確認純化的PRV vhs重組蛋白具有RNase活性且其降解能力，且不受RNA二級結構的影響。不同於HSV-1，PRV vhs不具此IRES特異性和五端往三端的方向性。除RNA外，本實驗首次發現PRV vhs具有類似RNase H的活性：可分解RNA-DNA hybrid。PRV vhs蛋白的RNase活性不會受RNA是否具有五端cap或三端poly(A)結構的影響，同樣可降解mRNA和rRNA，且當與eIF4B和eIF4H共同作用時會促進PRV vhs活性。
在in vivo的實驗中， PRV與HSV-1的vhs皆可抑制細胞內的蛋白表現，此作用主要是透過vhs分解RNA的能力所致。若將PRV vhs蛋白上的四個保留區其中任一個造成缺損，即會使PRV vhs失去抑制細胞內的蛋白表現的RNase activity。 此外，PRV box 3內的T172胺基酸(於HSV-1vhs對應的位置為T214) 和box 4內的352、356胺基對PRV vhs的的活性都有決定性的影響，為其活性決定位(key site)之一。
未來可就PRV vhs蛋白是否具有其他核醣核酸酶活性(例如：Fen-1)進行分析，或利用胺基酸比對結果，配合蛋白質構型分析結果選擇最有可能的胺基酸進行分析，需尋找其他PRV vhs的活性決定位。|
Pseudorabies virus (PRV) belongs to the alpha-herpesvirinae; the best characterized virus is herpes simplex virus type 1 (HSV-1). UL41 gene encodes vhs (virion host shutoff) protein that is highly conserved in alpha -herpesvirinae. Previous studies showed HSV-1 vhs harbors ribonuclease activity that contributes to the shutoff of protein synthesis in infected cells via mRNA degradation. HSV-1 vhs selectively decays the region near translation initiation and proceeds in an overall 5- to -3 direction. Moreover, vhs-induced RNA cleavage events is also affected by RNA structure; HSV-1 vhs cleavages RNA at sequences immediately 3 to the Internal Ribosome Entry Site (IRES). Reads and Smiley groups showed that HSV-1 vhs selectively targets actively translated mRNAs through interactions with eIF4F components, i.e. eIF4H, eIF4B, and eIF4A. Up to now the function of PRV vhs is poorly understood. Due to the low sequence similarity (as low as 39.3%), vhs proteins of HSV and PRV might share different biochemistry characteristics. Hence, the main goal of our study was set to explore the mechanisms of PRV vhs on the RNase hydrolysis and translational regulation. To do so, vhs was expressed and purified from E. coli. In vitro vhs assay indicated that PRV vhs indeed exerted RNase activity, 70% RNA was degraded after 40 min incubation and also degraded IRES structure. Interestingly, not only mRNA but also rRNA, PRV vhs degraded RNA/DNA hybrid that was shown for the first time. Different from HSV-1, RNA decay mediated by PRV vhs didn't show specific direction and didn't preferentially target at the region at 3 end of IRES. As HSV, PRV vhs ribonuclease activity was significant enhanced by addition of eIF4H and 4B proteins. Moreover in vivo assay demonstrated that each of four highly conserved boxes of vhs contributed to shutoff of protein synthesis via degradation of reporter RNA. Moreover, the dominant negative residue T172 (found in HSV-1 214), and 352, and 356 residues in box IV was the key site for PRV vhs ribonulease activity.
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