Functional role of the cytoplasmic tail domain of the major envelope fusion protein of group ii baculoviruses
文献类型：期刊论文
| 作者 | Long, Gang; Pan, Xiaoyu; Westenberg, Marcel; Vlak, Just M. |
| 刊名 | Journal of virology
 |
| 出版日期 | 2006-11-01 |
| 卷号 | 80期号:22页码:11226-11234 |
| ISSN号 | 0022-538X |
| DOI | 10.1128/jvi.01178-06 |
| 通讯作者 | Vlak, just m.(just.vlak@wur.nl) |
| 英文摘要 | F proteins from baculovirus nucleopolyhedrovirus (npv) group ii members are the major budded virus (bv) viral envelope fusion proteins. they undergo furin-like proteolysis processing in order to be functional. f proteins from different baculovirus species have a long cytoplasmic tail domain (ctd), ranging from 48 (spodoptera litura multicapsid npv [mnpv]) to 78 (adoxophyes honmai npv) amino acid (aa) residues, with a nonassigned function. this ctd is much longer than the ctd of gp64-like envelope fusion proteins (7 aa), which appear to be nonessential for bv infectivity. here we have investigated the functional role of the ctd of helicoverpa armigera single-capsid npv (hearnpv), a group ii npv. we combined a newly constructed hearnpv f-null bacmid knockout-repair system and an autographa californica mnpv (acmnpv) gp64-null bacmid knockout-pseudotype system with mutation and rescue experiments to study the functional role of the baculovirus f protein ctd. we show that except for the 16 c-terminal aa, the hearnpv f ctd is essential for virus spread from cell to cell. in addition, the ctd of hearnpv f is involved in bv production in a length-dependent manner and is essential for bv infectivity. the tyrosine residue y658, located 16 aa from the c terminus, seems to be critical. however, hearnpv f without a ctd still rescues the infectivity of gp64-null acmnpv bv, indicating that the ctd is not involved in processing and fusogenicity. altogether, our results indicate that the f protein is essential for baculovirus bv infectivity and that the ctd is important for f protein incorporation into bv. |
| WOS关键词 | CALIFORNICA MULTICAPSID NUCLEOPOLYHEDROVIRUS ; VIRUS ENV PROTEIN ; MEMBRANE-FUSION ; TRANSMEMBRANE PROTEIN ; CELL-SURFACE ; R-PEPTIDE ; GLYCOPROTEIN ; IDENTIFICATION ; TRUNCATION ; CLEAVAGE |
| WOS研究方向 | Virology |
| WOS类目 | Virology |
| 语种 | 英语 |
| WOS记录号 | WOS:000241821300031 |
| 出版者 | AMER SOC MICROBIOLOGY |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2375272 |
| 专题 | 武汉病毒研究所 |
| 通讯作者 | Vlak, Just M. |
| 作者单位 | 1.Univ Wageningen & Res Ctr, Dept Virol, NL-6709 PD Wageningen, Netherlands 2.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Long, Gang,Pan, Xiaoyu,Westenberg, Marcel,et al. Functional role of the cytoplasmic tail domain of the major envelope fusion protein of group ii baculoviruses[J]. Journal of virology,2006,80(22):11226-11234. |
| APA | Long, Gang,Pan, Xiaoyu,Westenberg, Marcel,&Vlak, Just M..(2006).Functional role of the cytoplasmic tail domain of the major envelope fusion protein of group ii baculoviruses.Journal of virology,80(22),11226-11234. |
| MLA | Long, Gang,et al."Functional role of the cytoplasmic tail domain of the major envelope fusion protein of group ii baculoviruses".Journal of virology 80.22(2006):11226-11234. |
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来源：武汉病毒研究所
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