|
|
|
题名
|
作者
|
年代
|
出处
|
被引量
|
| 1 | Insights into the function of tegument proteins from the varicella zoster virus显示文摘Chickenpox(varicella) is caused by primary infection with varicella zoster virus(VZV), which can establish long-term latency in the host ganglion. Once reactivated, the virus can cause shingles(zoster) in the host. VZV has a typical herpesvirus virion structure consisting of an inner DNA core, a capsid, a tegument, and an outer envelope. The tegument is an amorphous layer enclosed between the nucleocapsid and the envelope, which contains a variety of proteins. However, the types and functions of VZV tegument proteins have not yet been completely determined. In this review, we describe the current knowledge on the multiple roles played by VZV tegument proteins during viral infection. Moreover, we discuss the VZV tegument protein-protein interactions and their impact on viral tissue tropism in SCID-hu mice. This will help us develop a better understanding of how the tegument proteins aid viral DNA replication, evasion of host immune response, and pathogenesis. | WANG Wei CHENG Tong ZHU Hua XIA NingShao | 2015 | Science China(Life Sciences)2015,58,8: | 7 |
| 2 | HSV-1 stimulation-related protein HSRG1 inhibits viral gene transcriptional elongation by interacting with Cyclin T2显示文摘The protein encoded by HSRG1(HSV-1 stimulation-related gene 1) is a virally induced protein expressed in HSV-1-infected cells.We have already reported that HSRG1 is capable of interacting with transcriptional regulator proteins.To further analyze the effects of HSRG1 on the regulation of viral gene transcription,we expressed the HSRG1 protein in transfected cells and found that it postpones the proliferation of HSV-1.CAT(chloramphenicol acetyltransferase) assays also revealed that HSRG1 reduces transcription from HSV-1 promoters.Yeast two-hybrid and immunoprecipitation assays indicated that HSRG1 interacts with Cyclin T2,the regulatory subunit of P-TEFb,which is required for transcription elongation by RNA Pol II(RNAP II) ,and that amino acid residues 1-420 in Cyclin T2 are important for binding with HSRG1.Fluorescence assays suggested that the cellular localizations of those two proteins are influenced by their interaction.Further analyses with CAT assays revealed that HSRG1 inhibits the transcriptional activation by Cyclin T2 of viral promoters.Our results suggested that the inhibitory effects of HSRG1 on viral replication and proliferation are probably induced by its binding to Cyclin T2.Therefore,it is likely that HSRG1 inhibits viral gene transcriptional elongation by interacting with Cyclin T2. | WU WenJuan YU Xian LI WeiZhong GUO Lei LIU LongDing WANG LiChun LI QiHan | 2011 | Science China(Life Sciences)2011,54,4: | 3 |
| 3 | A cellular response protein induced during HSV-1 infection inhibits viral replication by interacting with ATF5显示文摘Studies of herpes simplex virus type 1(HSV-1)infection have shown that many known and unknown cellular molecules involved in viral proliferation are up-regulated following HSV-1 infection.In this study,using two-dimensional polyacrylamide gel electrophoresis,we found that the expression of the HSV-1 infection response repressive protein(HIRRP,GI 16552881)was up-regulated in human L02 cells infected with HSV-1.HIRRP,an unknown protein,was initially localized in the cytoplasm and then translocated into the nucleus of HSV-1-infected cells.Further analysis showed that HIRRP represses HSV-1proliferation by inhibiting transcription of the viral genome by interacting with the cellular transcription factor,ATF5,via its N-terminal domain.ATF5 represses the transcription of many host genes but can also act as an activator of genes containing a specific motif.We found that ATF5 promotes the proliferation of HSV-1 via a potential mechanism by which ATF5 enhances the transcription of viral genes during the course of an HSV-1 infection;HIRRP then induces feedback repression of this transcription by interacting with ATF5. | WU LianQiu ZHANG XueMei CHE YanChun ZHANG Ying TANG SongQing LIAO Yun NA RuiXiong XIONG XiangLin LIU LongDing LI QiHan | 2013 | Science China(Life Sciences)2013,56,12: | 2 |
| 4 | A Multiple Functional Protein:the Herpes Simplex Virus Type 1 Tegument Protein VP22显示文摘The herpes simplex virus type 1(HSV-1) VP22,is one of the most abundant HSV-1 tegument proteins with an average stoichiometry of 2 400 copies per virion and conserved among alphaherpesvirinae. Many functions are attributed to VP22,including nuclear localization,chromatin binding,microtubule binding,induction of microtubule reorganization,intercellular transport,interaction with cellular proteins,such as template activating factor I(TAF-I) and nonmuscle myosin II A(NMIIA) ,and viral proteins including tegument protein VP16,pUS9 and pUL46,glycoprotein E(gE) and gD. Recently,many novel functions performed by the HSV-1 VP22 protein have been shown,including promotion of protein synthesis at late times in infection,accumulation of a subset of viral mRNAs at early times in infection and possible transcriptional regulation function. | Mei-li LI Hong GUO Qiong DING Chun-fu ZHENG | 2009 | Virologica Sinica2009,24,3: | 0 |