Mutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein
文献类型：期刊论文
| 作者 | Tan, Ying1,2,4; Jiang, Ling3; Wang, Manli1,2,4; Yin, Feifei1,2,4; Deng, Fei1,2; Liu, Maili3; Hu, Zhihong1,2; Wang, Hualin1,2 |
| 刊名 | JOURNAL OF VIROLOGY
 |
| 出版日期 | 2008-08-01 |
| 卷号 | 82期号:16页码:8138-8148 |
| 英文摘要 | The entry of enveloped viruses into cells is normally mediated by fusion between viral and cellular membranes, in which the fusion peptide plays a crucial role. The fusion peptides of group II nucleopolyhedrovirus (NPV) F proteins are quite conserved, with a hydrophobic region located at the N terminal of the F(1) fragment. For this report, we used mutagenesis and nuclear magnetic resonance (NMR) to study the structure and function of the fusion peptide of the Helicoverpa armigera single-nucleocapsid NPV (HearNPV) F protein (HaF). Five mutations in the fusion peptide of HaF, N(1)G, N(1)L, I(2)N, G(3)L, and D(11)L, were generated separately, and the mutated f genes were transformed into the f-null HearNPV bacmid. The mutations N(1)L, I(2)N, and D(11)L were found to completely abolish the ability of the recombinant bacmids to produce infectious budded virus, while the mutations N(1)G and G(3)L did not. The low-pH-induced envelope fusion assay demonstrated that the N(1)G substitution increased the fusogenicity of HaF, while the G(3)L substitution reduced its fusogenicity. NMR spectroscopy was used to determine the structure of a synthetic fusion peptide of HaF in the presence of sodium dodecyl sulfate micelles at pH 5.0. The fusion peptide appeared to be an amphiphilic structure composed of a flexible coil in the N terminus from N(1) to N(5), a 3(10)-helix from F(6) to G(8), a turn at S(9), and a regular alpha-helix from V(10) to D(19). The data provide the first NMR structure of a baculovirus fusion peptide and allow us to further understand the relationship of structure and function of the fusion peptide. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Virology |
| 研究领域[WOS] | Virology |
| 关键词[WOS] | VIRUS MEMBRANE-FUSION ; INFLUENZA HEMAGGLUTININ ; BACULOVIRUS GP64 ; FUNCTIONAL-ANALYSIS ; CONSERVED GLYCINE ; DOMAIN ; ENTRY ; CELLS ; MECHANISM ; PROGRAM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000258166500037 |
| 公开日期 | 2015-10-20 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/8126]  |
| 专题 | 武汉物理与数学研究所_2011年以前论文发表（包括2011年） |
| 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, Wuhan Inst Phys & Math, State Key Lab Magnet Resonance & Atom & Mol Phys, Wuhan 430071, Peoples R China 4.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Tan, Ying,Jiang, Ling,Wang, Manli,et al. Mutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein[J]. JOURNAL OF VIROLOGY,2008,82(16):8138-8148. |
| APA | Tan, Ying.,Jiang, Ling.,Wang, Manli.,Yin, Feifei.,Deng, Fei.,...&Wang, Hualin.(2008).Mutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein.JOURNAL OF VIROLOGY,82(16),8138-8148. |
| MLA | Tan, Ying,et al."Mutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein".JOURNAL OF VIROLOGY 82.16(2008):8138-8148. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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