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	The putative pocket protein binding site of autographa californica nucleopolyhedrovirus bv/odv-c42 is required for virus-induced nuclear actin polymerization
	Li, Kun1,2; Wang, Yun1; Bai, Huimin1,2; Wang, Qian1; Song, Jianhua1; Zhou, Yuan1; Wu, Chunchen1; Chen, Xinwen1
刊名	Journal of virology
	2010-08-01
卷号	84期号:15页码:7857-7868
ISSN号	0022-538X
DOI	10.1128/jvi.00174-10
通讯作者	Chen, xinwen(chenxw@pentium.whiov.ac.cn)
英文摘要	Nuclear filamentous actin (f-actin) is essential for nucleocapsid morphogenesis of lepidopteran nucleopolyhedroviruses. previously, we had demonstrated that autographa californica multiple nucleopolyhedrovirus (acmnpv) bv/odv-c42 (c42) is involved in nuclear actin polymerization by recruiting p78/83, an acmnpv orf9-encoded n-wasp homology protein that is capable of activating an actin-related-protein 2/3 (arp2/3) complex to initiate actin polymerization, to the nucleus. to further investigate the role of c42 in virus-induced actin polymerization, the recombinant bacmid vac(p78/83nls-gfp), with a c42 knockout, p78/83 tagged with a nuclear localization signal coding sequence, and egfp as a reporter gene under the control of the pp10 promoter, was constructed and transfected to sf9 cells. in the nuclei of vac(p78/83nls-gfp)-transfected cells, polymerized f-actin filaments were absent, whereas other actin polymerization elements (i.e., p78/83, g-actin, and arp2/3 complex) were present. this in vivo evidence indicated that c42 actively participates in the nuclear actin polymerization process as a key element, besides its role in recruiting p78/83 to the nucleus. in order to collect in vitro evidence for the participation of c42 in actin polymerization, an anti-c42 antibody was used to neutralize the viral nucleocapsid, which is capable of initiating actin polymerization in vitro. both the kinetics of pyrene-actin polymerization and f-actin-specific staining by phalloidin indicated that anti-c42 can significantly attenuate the efficiency of f-actin formation compared to that with control antibodies. furthermore, we have identified the putative pocket protein binding sequence (ppbs) on c42 that is essential for c42 to exert its function in nuclear actin polymerization.
WOS关键词	HELICOVERPA-ARMIGERA NUCLEOPOLYHEDROVIRUS ; OCCLUSION-DERIVED VIRUS ; OPEN READING FRAME ; ARP2/3 COMPLEX ; POLYHEDROSIS-VIRUS ; RETINOBLASTOMA PROTEIN ; N-WASP ; LISTERIA-MONOCYTOGENES ; STRUCTURAL PROTEIN ; CYTOCHALASIN-D
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:000279989800043
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2375717
专题	武汉病毒研究所
通讯作者	Chen, Xinwen
作者单位	1.Chinese Acad Sci, State Key Lab Virol, Wuhan Inst Virol, Wuhan 430071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Li, Kun,Wang, Yun,Bai, Huimin,et al. The putative pocket protein binding site of autographa californica nucleopolyhedrovirus bv/odv-c42 is required for virus-induced nuclear actin polymerization[J]. Journal of virology,2010,84(15):7857-7868.
APA	Li, Kun.,Wang, Yun.,Bai, Huimin.,Wang, Qian.,Song, Jianhua.,...&Chen, Xinwen.(2010).The putative pocket protein binding site of autographa californica nucleopolyhedrovirus bv/odv-c42 is required for virus-induced nuclear actin polymerization.Journal of virology,84(15),7857-7868.
MLA	Li, Kun,et al."The putative pocket protein binding site of autographa californica nucleopolyhedrovirus bv/odv-c42 is required for virus-induced nuclear actin polymerization".Journal of virology 84.15(2010):7857-7868.

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