Expression of Human Cytomegalovirus IE1 Leads to Accumulation of Mono-SUMOylated PML That Is Protected from Degradation by Herpes Simplex Virus 1 ICP0
文献类型：期刊论文
| 作者 | Tang, Qiyi4; Luo, Min-Hua5; Reeves, Inez2; Ahn, Jin-Hyun3; Wen, Fayuan4; Cruz-Cosme, Ruth4; Hou, Wangheng1,4 |
| 刊名 | JOURNAL OF VIROLOGY
 |
| 出版日期 | 2018-12-01 |
| 卷号 | 92期号:23页码:12 |
| ISSN号 | 0022-538X |
| 关键词 | cytomegalovirus (CMV) immediate-early protein 1 (IE1) herpes simplex virus (HSV) infected cellular protein (ICP0) promyelocytic leukemia protein (PML) nuclear domain 10 (ND10) SUMOylation HSV-1 |
| DOI | 10.1128/JVI.01452-18 |
| 英文摘要 | To countermeasure the host cellular intrinsic defense, cytomegalovirus (CMV) and herpes simplex viruses (HSV) have evolved the ability to disperse nuclear domain 10 (ND10, aka PML body). However, mechanisms underlying their action on ND10 differ. HSV infection produces ICP0, which degrades the ND10-forming protein PML. Human CMV (HCMV) infection expresses IE1 that deSUMOylates PML to result in dispersion of ND10. It has been demonstrated that HSV ICP0 degraded only the SUMOylated PML, so we hypothesized that HCMV 1E1 can protect PML from degradation by ICP0. HCMV IE1-expressing cell lines (U-251 MG-IE1 and HELF-IE1) were used for infection of HSV-1 or transfection of ICP0-expressing plasmid. Multilabeling by immunocytochemistry assay and protein examination by Western blot assay were performed to determine the resultant fate of PML caused by ICP0 in the presence or absence of HCMV IE1. Here, we report that deSUMOylation of human PML (hPML) by HCMV IE1 was incomplete, as mono-SUMOylated PML remained in the IE1-expressing cells, which is consistent with the report by E. M. Schilling, M. Scherer, N. Reuter, J. Schweininger, et al. (J Virol 91:e02049-16, 2017, https://doi.org/10.1128/JVI.02049-16). As expected, we found that IE1 protected PML from degradation by ICP0 or HSV-1 infection. An in vitro study found that IE1 with mutation of L174P failed to deSUMOylate PML and did not protect PML from degradation by ICP0; hence, we conclude that the deSUMOylation of PML is important for IE1 to protect PML from degradation by ICP0. In addition, we revealed that murine CMV failed to deSUMOylate and to protect the HSV-mediated degradation of hPML, and that HCMV failed to deSUMOylate and protect the HSV-mediated degradation of mouse PML. However, IE1-expressing cells did not enhance wild-type HSV-1 replication but significantly increased ICP0-defective HSV-1 replication at a low multiplicity of infection. Therefore, our results uncovered a host-virus functional interaction at the posttranslational level. IMPORTANCE Our finding that HCMV IE1 protected hPML from degradation by HSV ICP0 is important, because the PML body (aka ND10) is believed to be the first line of host intrinsic defense against herpesviral infection. How the infected viruses overcome the nuclear defensive structure (PML body) has not been fully understood. Herpesviral proteins, ICP0 of HSV and IE1 of CMV, have been identified to interact with PML. Here, we report that HCMV IE1 incompletely deSUMOylated PML, resulting in the mono-SUMOylated PML, which is consistent with the report of Schilling et al. (J Virol 91:e02049-16, 2017, https://doi.org/10.1128/JVI.02049-16). The mono-SUMOylated PML was subjected to degradation by HSV ICP0. However, it was protected by 1E1 from degradation by ICP0 or HSV-1 infection. In contrast, IE1 with L174P mutation lost the function of deSUMOylating PML and failed to protect the degradation of the mono-SUMOylated PML. Whether the mono-SUMOylated PML has any defensive function against viral infection will be further investigated. |
| 资助项目 | NIH/NIAID[SC1AI112785] ; National Natural Science Foundation of China[81701999] ; National Institute on Minority Health and Health Disparities of the National Institutes of Health[G12MD007597] |
| WOS研究方向 | Virology |
| 语种 | 英语 |
| 出版者 | AMER SOC MICROBIOLOGY |
| WOS记录号 | WOS:000450002000031 |
| 源URL | [http://202.127.146.157/handle/2RYDP1HH/6063]  |
| 专题 | 中国科学院武汉植物园 |
| 通讯作者 | Tang, Qiyi |
| 作者单位 | 1.Xiamen Univ, Sch Publ Hlth, Natl Inst Diagnost & Vaccine Dev Infect Dis, State Key Lab Mol Vaccinol & Mol Diagnost, Xiamen, Peoples R China 2.Howard Univ, Coll Med, Dept Obstet & Gynecol, Div Neonatol, Washington, DC USA 3.Sungkyunkwan Univ, Sch Med, Samsung Med Ctr, Dept Mol Cell Biol, Suwon, South Korea 4.Howard Univ, Coll Med, Dept Microbiol, Washington, DC 20059 USA 5.Chinese Acad Sci, Wuhan Inst Virol, CEBSIT, State Key Lab Virol, Wuhan, Hubei, Peoples R China |
| 推荐引用方式 GB/T 7714 | Tang, Qiyi,Luo, Min-Hua,Reeves, Inez,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]. JOURNAL OF VIROLOGY,2018,92(23):12. |
| APA | Tang, Qiyi.,Luo, Min-Hua.,Reeves, Inez.,Ahn, Jin-Hyun.,Wen, Fayuan.,...&Hou, Wangheng.(2018).Expression of Human Cytomegalovirus IE1 Leads to Accumulation of Mono-SUMOylated PML That Is Protected from Degradation by Herpes Simplex Virus 1 ICP0.JOURNAL OF VIROLOGY,92(23),12. |
| MLA | Tang, Qiyi,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".JOURNAL OF VIROLOGY 92.23(2018):12. |
入库方式： OAI收割
来源：武汉植物园
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