Six-helix bundle assembly and characterization of heptad repeat regions from the F protein of Newcastle disease virus

文献类型： 外文期刊

第一作者： Yu, M

作者： Yu, M;Wang, EX;Liu, YF;Cao, DJ;Jin, NY;Zhang, CWH;Bartlam, M;Rao, ZH;Tien, P;Gao, GF

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期刊名称：JOURNAL OF GENERAL VIROLOGY （ 影响因子：3.891； 五年影响因子：3.719 ）

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收录情况： SCI

摘要： Paramyxoviruses may adopt a similar fusion mechanism to other enveloped viruses, in which an antiparallel six-helix bundle structure is formed post-fusion in the heptad repeat (HR) regions of the envelope fusion protein. In order to understand the fusion mechanism and identify fusion inhibitors of Newcastle disease virus (NDV), a member of the Paramyxoviridae family, we have developed an E. coli system that separately expresses the F protein HR1 and HR2 regions as GST fusion proteins. The purified cleaved HR1 and HR2 have subsequently been assembled into a stable six-helix bundle heterotrimer complex. Furthermore, both the GST fusion protein and the cleaved HR2 show virus-cell fusion inhibition activity (IC50 of 1.07-2.93 muM). The solubility of the GST-HR2 fusion protein is much higher than that of the corresponding peptide. Hence this provides a plausible method for large-scale production of HR peptides as virus fusion inhibitors. [References: 26]

分类号： R37`R373

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