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

Dept of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People’s Republic of China¹
Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, People’s Republic of China²
Dept of Virus Research, University of Military Supplies, Changchun 130062, People’s Republic of China³
Laboratory of Immunobiology, Dana-Farber Cancer Institute and Dept of Medicine, Harvard Medical School, Boston, MA 02115, USA⁴
Laboratory of Structural Biology and MOE Laboratory of Protein Sciences, Tsinghua University, Beijing 100084, People’s Republic of China⁵
Laboratory of Molecular Medicine, Children’s Hospital, Dept of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, and Dept of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA⁶

Authors for correspondence: (i) George Gao. Present address: Room 7508, Nuffield Dept of Clinical Medicine, John Radcliffe Hospital, University of Oxford, Headington, Oxford OX3 9DU, UK. Fax +44 1865 220993. e-mail ggao66{at}yahoo.com (ii) Po Tien. e-mail tienpo@sun.im.ac.cn

Paramyxoviruses may adopt a similar fusion mechanism to other enveloped viruses, in which an anti-parallel 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 µM). 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.

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