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Autographa californica multiple nucleopolyhedrovirus nucleocapsid protein bv/odv-c42 mediates the nuclear entry of p78/83
Wang, Yun1,2; Wang, Qian1; Liang, Changyong1; Song, Jianhua1; Li, Ni1,2; Shi, Hui1,2; Chen, Xinwen1
刊名Journal of virology
2008-05-01
卷号82期号:9页码:4554-4561
ISSN号0022-538X
DOI10.1128/jvi.02510-07
通讯作者Chen, xinwen(chenxw@pentium.whiov.ac.cn)
英文摘要Autographa californica multiple nucleopolyhedrovirus (acmnpv) bv/odv-c42 (orf101; c42), which encodes a 41.5-kda viral nucleocapsid protein with a putative nuclear localization signal (nls) motif at the c terminus, is a highly conserved gene among members of the baculoviridae family. c42 is demonstrated to be essential for acmnpv propagation and can bind to nucleocapsid protein p78/83, a viral activator for the actin-related protein 2/3 (arp2/3) complex to initiate nuclear actin polymerization, which is essential for viral nucleocapsid morphogenesis during acmnpv infection. here, we report the identification of a novel pathway through which c42 functions in nucleocapsid assembly. cotransfection of sf9 cells with c42 and p78/83 plasmids demonstrated that c42 was capable of recruiting p78/83 to the nuclei of uninfected cells and that the nls motif of c42 was essential for this process. to validate this nuclear relocation mode in bacmid-transfected cells, a c42-disrupted bacmid (vac(c42ko-gfp)) and rescued bacmids with wild-type c42 (vacc42(res-gfp)) or with nls coding sequencemutated c42 (vacc42(nls-gfp)) were prepared. by immuno-staining, p78/83 was found to be localized in the cytoplasm of either vac(c421ko-gfp) - or vac(c42nls-gfp)-transfected cells, whereas p78/83 was relocated to the nuclei of vac(c42res-gfp)-transfected cells. furthermore, f-actin-specific staining confirmed that there was no actin polymerization activity in the nuclei of either vac(c42ko-gfp) - or vav(c42nls-gfp)-transfected cells, which might be attributed to the absence of nuclear p78/83, an activator of the arp2/3 complex to initiate nuclear actin polymerization. we therefore hypothesize a mode of action where c42 binds to p78/83 in the cytoplasm to form a protein complex and cotransports to the nucleus under the direction of the nls motif in c42 during acmnpv infection.
WOS关键词OPEN READING FRAME ; MULTICAPSID NUCLEOPOLYHEDROVIRUS ; ESCHERICHIA-COLI ; ACTIN ; EXPRESSION ; GENE ; IDENTIFICATION ; PHOSPHOPROTEIN ; BACULOVIRUSES ; LOCALIZATION
WOS研究方向Virology
WOS类目Virology
语种英语
出版者AMER SOC MICROBIOLOGY
WOS记录号WOS:000255084600036
内容类型期刊论文
URI标识http://www.corc.org.cn/handle/1471x/2375485
专题武汉病毒研究所
通讯作者Chen, Xinwen
作者单位1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
推荐引用方式
GB/T 7714
Wang, Yun,Wang, Qian,Liang, Changyong,et al. Autographa californica multiple nucleopolyhedrovirus nucleocapsid protein bv/odv-c42 mediates the nuclear entry of p78/83[J]. Journal of virology,2008,82(9):4554-4561.
APA Wang, Yun.,Wang, Qian.,Liang, Changyong.,Song, Jianhua.,Li, Ni.,...&Chen, Xinwen.(2008).Autographa californica multiple nucleopolyhedrovirus nucleocapsid protein bv/odv-c42 mediates the nuclear entry of p78/83.Journal of virology,82(9),4554-4561.
MLA Wang, Yun,et al."Autographa californica multiple nucleopolyhedrovirus nucleocapsid protein bv/odv-c42 mediates the nuclear entry of p78/83".Journal of virology 82.9(2008):4554-4561.
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