中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
The f protein of helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from spodoptera exigua multiple nucleopolyhedrovirus

文献类型:期刊论文

作者Wang, Manli1,2,3; Tan, Ying1,2,3; Yin, Feifei1,2,3; Deng, Fei1,2; Vlak, Just M.4; Hu, Zhihong1,2; Wang, Hualin1,2
刊名Journal of general virology
出版日期2008-03-01
卷号89页码:791-798
ISSN号0022-1317
DOI10.1099/vir.0.83466-0
通讯作者Wang, hualin(h.wang@wh.iov.cn)
英文摘要F proteins of group ii nucleopolyhedroviruses (npvs) are envelope fusion proteins essential for virus entry and egress. an f-null helicoverpa armigera single nucleocapsid npv (hearnpv) bacmid, habac delta f, was constructed. this bacmid could not produce infectious budded virus (bv) when transfected into hzam1 cells, showing that f protein is essential for cell-to-cell transmission of bvs. when habac delta f was pseudotyped with the homologous f protein (habac delta f-haf, positive control) or with the heterologous f protein from spodoptera exigua multinucleocapsid npv (semnpv) (habac delta f-sef), infectious bvs were produced with similar kinetics. in the late phase of infection, the bv titre of habac delta f-sef virus was about ten times lower than that of habac delta f-haf virus. both pseudotyped viruses were able to fuse hzam1 cells in a similar fashion. the f proteins of both hearnpv and semnpv were completely cleaved into f, and f2 in the bvs of vhabac delta f-haf and vhabac delta f-sef, respectively, but the cleavage of sef in vhabac delta f-sef- infected hzam1 cells was incomplete, explaining the lower bv titre of vhabac delta f-sef. polyclonal antisera against haf(1) and sef1 specifically neutralized the infection of vhabac delta f-haf and vhabac delta f-sef, respectively. haf(1) antiserum showed some cross-neutralization with vhabac delta f-sef. these results demonstrate that group ii npv f proteins can be functionally replaced with a homologue of other group ii npvs, suggesting that the interaction of f with other viral or host proteins is not absolutely species-specific.
WOS关键词ENVELOPE FUSION PROTEIN ; CALIFORNICA MULTICAPSID NUCLEOPOLYHEDROVIRUS ; NUCLEAR POLYHEDROSIS-VIRUS ; BACULOVIRUS GP64 ; MEMBRANE-FUSION ; FURIN ; CLEAVAGE ; SEQUENCE ; OLIGOMERIZATION ; IDENTIFICATION
WOS研究方向Biotechnology & Applied Microbiology ; Virology
WOS类目Biotechnology & Applied Microbiology ; Virology
语种英语
WOS记录号WOS:000253998700021
出版者SOC GENERAL MICROBIOLOGY
URI标识http://www.irgrid.ac.cn/handle/1471x/2375513
专题武汉病毒研究所
通讯作者Wang, Hualin
作者单位1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Wuhan Inst Virol, Joint Lab Invertebrate Virol, Wuhan 430071, Peoples R China
3.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
4.Wageningen Univ, Virol Lab, NL-6709 PD Wageningen, Netherlands
推荐引用方式
GB/T 7714
Wang, Manli,Tan, Ying,Yin, Feifei,et al. The f protein of helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from spodoptera exigua multiple nucleopolyhedrovirus[J]. Journal of general virology,2008,89:791-798.
APA Wang, Manli.,Tan, Ying.,Yin, Feifei.,Deng, Fei.,Vlak, Just M..,...&Wang, Hualin.(2008).The f protein of helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from spodoptera exigua multiple nucleopolyhedrovirus.Journal of general virology,89,791-798.
MLA Wang, Manli,et al."The f protein of helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from spodoptera exigua multiple nucleopolyhedrovirus".Journal of general virology 89(2008):791-798.

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来源:武汉病毒研究所

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