Institute of Pathogenic Biology, University of South China Key Laboratory of Prevention and Control of Special Pathogens in Hunan Province,Hengyang 421001,China
Abstract：Death domain-associated protein is a multifunctional protein, which can participate in apoptosis, anti-virus and other activities. When virus infection occurs, some protein expressed by viruses can interact with Daxx, and play a positive or negative role in the anti-virus response from Daxx by different pathways. The interaction of Daxx with the protein from different virus or even different protein from the same virus will involve in different inhibition or promotion. A brief overview about the effects on the interaction of Daxx with proteins expressed by some DNA viruses, such as human adenovirus, human cytomegalovirus, human papillomavirus (HPV) and etc.
丁霜,唐双阳,杨晓东,申海艳,万艳平. 死亡结构域蛋白Daxx与DNA病毒蛋白相互作用及影响的研究进展[J]. 中国人兽共患病学报, 2020, 36(3): 239-244.
DING Shuang,TANG Shuang-yang,YANG Xiao-dong,SHEN Hai-yan,WAN Yan-ping. Research advances on interaction of Daxx with DNA viral proteins. Chinese Journal of Zoonoses, 2020, 36(3): 239-244.
[1] Yang X, Khosravi-Far R, Chang HY, et al. Daxx, a novel Fas-binding protein that activates JNK and apoptosis[J]. Cell, 1997, 89(7):1067-1076. DOI:10.1016/S0092-8674(00)80294-9 [2] Guion L,Bienkowska-Haba M,DiGiuseppe S,et al. PML nuclear body-residing proteins sequentially associate with HPV genome after infectious nuclear delivery[J]. PLoS Pathog, 2019, 15(2):e100759. DOI: 10.1371/journal.ppat.1007590 [3] Shastrula PK, Sierra I, Deng Z, et al. PML is recruited to heterochromatin during S phase and represses DAXX-mediated histone H3.3 chromatin assembly[J]. J Cell Sci, 2019,132(6):jcs220970. DOI: 10.1242/jcs.220970 [4] Li Q,Wang J,Liao D,et al. Degradation of DAXX by adenovirus type 12 E1B-55K circumvents chemoresistance of ovarian cancer to cisplatin[J]. Virology, 2018, 521:118-128. DOI: 10.1016/j.virol. 2018.05.026 [5] Wimmer P, Blanchette P, Schreiner S, et al. Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein[J]. Oncogene, 2013, 32(13):1626-1637.DOI: 10.1038/ onc.2012.187 [6] Müncheberg S, Hay RT, Ip WH, et al. E1B-55K-mediated regulation of RNF4 SUMO-targeted ubiquitin ligase promotes human adenovirus gene expression[J]. J Virol, 2018, 92(13): e00164-18.DOI: 10.1128/ JVI.00164-18 [7] Schreiner S, Bürck C, Glass M, et al. Control of human adenovirus type 5 gene expression by cellular Daxx/ATRX chromatin-associated complexes[J]. Nucleic Acids Res, 2013, 41(6):3532-3550.DOI: 10.1093/ nar/gkt064 [8] Wang L, Liu X, Wang H, et al. RNF4 regulates zebrafish granulopoiesis through the DNMT1-C/EBPα axis[J]. FASEB J, 2018, 32(9):4930-4940.DOI: 10.1096/fj.201701450RR [9] Kang S, Kang D, Bakhtiar Ul Islam SM, et al. Silencing Daxx increases the anti-tumor activity of a TRAIL/shRNA Bcl-xL-expressing oncolytic adenovirus through enhanced viral replication and cellular arrest[J]. Cell Signal, 2015, 27(6):1214-1224.DOI: 10.1016/j.cellsig.2015.02.028 [10] Sohn SY, Hearing P. Mechanism of Adenovirus E4-ORF3-Mediated SUMO Modifications[J]. MBio, 2019, 10(1):e00022-19. DOI: 10.1128/mBio.00022-19 [11] Ullman AJ, Hearing P. Cellular proteins PML and Daxx mediate an innate antiviral defense antagonized by the adenovirus E4 ORF3 protein[J]. J Virol, 2008, 82(15):7325-7335. DOI: 10.1128/JVI.00723-08 [12] Vink EI, Zheng Y, Yeasmin R, et al. Impact of Adenovirus E4-ORF3 Oligomerization and Protein Localization on Cellular Gene Expression[J]. Viruses, 2015, 7(5):2428-2449. DOI: 10.3390/v7052428 [13] Xu P, Roizman B. The SP100 component of ND10 enhances accumulation of PML and suppresses replication and the assembly of HSV replication compartments[J]. Proc Natl Acad Sci USA,2017,114(19):3823-3829. DOI: 10.1073/pnas.1703395114 [14] Freudenberger N, Meyer T,Groitl P, et al. Human Adenovirus Core Protein V Is Targeted by the Host SUMOylation Machinery To Limit Essential Viral Functions[J]. J Virol, 2018,92(4):e01451-17. DOI: 10.1128/JVI.01451-17 [15] Vardi N, Chaturvedi S, Weinberger LS. Feedback-mediated signal conversion promotes viral fitness[J]. Proc Natl Acad Sci USA, 2018, 115(37):8803-8810. DOI: 10.1073/pnas.1802905115 [16] Ashley CL, Glass MS, Abendroth A, et al. Nuclear domain 10 components upregulated via interferon during human cytomegalovirus infection potently regulate viral infection[J]. J Gen Virol, 2017, 98(7):1795-1805. DOI: 10.1099/jgv.0.00085 [17] Wagenknecht N, Reuter N, Scherer M, et al. Contribution of the Major ND10 Proteins PML, hDaxx and Sp100 to the Regulation of Human Cytomegalovirus Latency and Lytic Replication in the Monocytic Cell Line THP-1[J]. Viruses, 2015, 7(6):2884-2907. DOI: 10.3390/v7062751 [18] Hwang J, Kalejta RF. In vivo analysis of protein sumoylation induced by a viral protein: Detection of HCMV pp71-induced Daxx sumoylation[J]. Methods, 2011, 55(2):160-165. DOI: 10.1016/j.ymeth.2011.07.004 [19] Winkler LL, Kalejta RF. The 19S proteasome activator promotes human cytomegalovirus immediate early gene expression through proteolytic and nonproteolytic mechanisms[J]. J Virol, 2014, 88(20):11782-11790. DOI: 10.1128/JVI.01720-14 [20] McFarlane S, Preston CM. Human cytomegalovirus immediate early gene expression in the osteosarcoma line U2OS is repressed by the cell protein ATRX[J]. Virus Res, 2011, 157(1):47-53. DOI: 10.1016/j.virusres. 2011.02.002 [21] Lu Y, Orr A, Everett RD. Stimulation of the replication of ICP0-Null mutant herpes simplex virus 1 and pp71-Deficient human cytomegalovirus by epstein-Barr virus tegument protein BNRF1[J]. J Virol, 2016, 90(21):9664-9673. DOI: 10.1128/JVI.01224-16 [22] Hou W, Cruz-Cosme R, Wen F, et al. Expression of human cytomegalovirus IE1 leads to accumulation of mono-SUMOylated PML that is protected from degradation by herpes simplex virus 1 ICP0[J]. J Virol, 2018, 92(23):e01452-18. DOI: 10.1128/JVI.01452-18 [23] Poole EL, Kew VG, Lau JCH,et al. A Virally Encoded DeSUMOylase Activity Is Required for Cytomegalovirus Reactivation from Latency[J]. Cell Rep, 2018, 24(3):594-606. DOI: 10.1016/j.celrep. 2018.06.048 [24] Reeves M, Woodhall D, Compton T, et al. Human cytomegalovirus IE72 protein interacts with the transcriptional repressor hDaxx to regulate LUNA gene expression during lytic infection[J]. J Virol, 2010, 84(14):7185-7194. DOI: 10.1128/JVI.02231-09 [25] Fuentes-GonzG AM,Munoz-Bello Jo,Manzo-Merino J,et al. Intratype variants of the E2 protein from human papillomavirus type 18 induce different gene expression profiles associated with apoptosis and cell proliferation[J]. Arch Virol, 2019, 164(7):1815-1827. DOI: 10.1007/S00705-019-04177-1 [26] Kivipold P, Vosa L, Ustav M, et al. DAXX modulates human papillomavirus early gene expression and genome replication in U2OS cells[J]. Virol J, 2015, 12:104. DOI: 10.1186/s12985-015-0335-z [27] Tang SY,Li L,Liu Y,et al. Interaction of DAXX and human papillomavirus type 16 E2 protein[J]. Mol Biol (Mosk), 2014, 48(4):682-686. DOI 10.1134/S0026893314040165 [28] 周蕾,张慧杰,黄成琳,等.Daxx和HPV16 E6在宫颈病变中的表达及其意义 [J].中华医学杂志,2015,95(37): 3050-3053. DOI: 10.3760/cma.j.issn.0376-2491.2015.37.012 [29] Namvar A, Bolhassani A, Hashemi M. HPV16 L2 improves HPV16 L1 gene delivery as an important approach for vaccine design against cervical cancer[J]. Bratisl Lek Listy, 2016, 117(3):179-184. DOI: 10.4149/BLL_2016_034 [30] Stepp WH, Meyers JM, McBride AA. Sp100 provides intrinsic immunity against human papillomavirus infection[J]. MBio, 2013, 4(6):e00845-13. DOI: 10.1128/mBio.00845-13 [31] Lukashchuk V,Everett RD. Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx[J]. J Virol, 2010, 84(8):4026-4040.DOI: 10.1128/JVI.02597-09 [32] Merkl PE, Orzalli MH, Knipe DM. Mechanisms of host IFI16, PML, and Daxx protein restriction of herpes simplex virus 1 replication[J]. J Virol, 2018, 92(10):e00057-18. DOI: 10.1128/JVI.00057-18 [33] Cohen C, Corpet A,Roubille S, et al. Promyelocytic leukemia (PML) nuclear bodies (NBs) induce latent/quiescent HSV-1 genomes chromatinization through a PML NB/Histone H3.3/H3.3 Chaperone Axis[J]. PLoS Pathog, 2018,14(9):e1007313. DOI: 10.1371/journal.ppat.1007313 [34] Kim JA, Choi MS, Min JS, et al. HSV-1 ICP27 represses NF-κB activity by regulating Daxx sumoylation[J]. BMB Reports, 2017, 50(5):275-280. DOI: 10.5483/bmbrep.2017.50.5.010 [35] De Leo A, Deng Z, Vladimirova O,et al. LANA oligomeric architecture is essential for KSHV nuclear body formation and viral genome maintenance during latency[J]. PLoS Pathog, 2019, 15(1):e1007489. DOI: 10.1371/journal.ppat.1007489 [36] Hahn AS, Grobkopf AK, Jungnickl D, et al. Viral Fragat homolog ORF75 of rhesus monkey rhadinovirus effects proteasomal degradation of the ND10 components SP100 and PML[J]. J Virol, 2016, 90(17):8013-8028. DOI: 10.1128/JVI.01181-16 [37] Huang H, Deng Z, Vladimirova O, et al. Structural basis underlying viral hijacking of a histone chaperone complex[J]. Nat Commun, 2016, 7:12707. DOI: 10.1038/ncomms12707 [38] Wei SC,Tsai CH,Hsu WT,et al. Baculovirus IE2 interacts with viral DNA through Daxx to generate an organized nuclear body structure for gene activation in vero cells[J]. J Virol, 2019, 93(8):e00149-19. DOI: 10.1128/JVI.00149-19 [39] Neumann F, Czech-Sioli M, Dobner T,et al. Replication of Merkel cell polyomavirus induces reorganization of promyelocytic leukemia nuclear bodies[J]. J Gen Virol, 2016, 97(11):2926-2938. DOI: 10.1099/jgv. 0.000593
2020, Vol. 36 
