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Journal of Virology, August 2008, p. 8138-8148, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.00368-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Mutagenesis and Nuclear Magnetic Resonance Analyses of the Fusion Peptide of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein{triangledown}

Ying Tan,1,3 Ling Jiang,2 Manli Wang,1,3 Feifei Yin,1,3 Fei Deng,1 Maili Liu,2 Zhihong Hu,1 and Hualin Wang1*

State Key Laboratory of Virology and Joint Laboratory of Invertebrate Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China,1 State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China,2 Graduate School of the Chinese Academy of Sciences, Beijing 100039, People's Republic of China3

Received 19 February 2008/ Accepted 28 May 2008

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 F1 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, N1G, N1L, I2N, G3L, and D11L, were generated separately, and the mutated f genes were transformed into the f-null HearNPV bacmid. The mutations N1L, I2N, and D11L were found to completely abolish the ability of the recombinant bacmids to produce infectious budded virus, while the mutations N1G and G3L did not. The low-pH-induced envelope fusion assay demonstrated that the N1G substitution increased the fusogenicity of HaF, while the G3L 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 N1 to N5, a 310-helix from F6 to G8, a turn at S9, and a regular {alpha}-helix from V10 to D19. 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.

* Corresponding author. Mailing address: Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China. Phone and fax: 86-27-87199353. E-mail: h.wang{at}wh.iov.cn

{triangledown} Published ahead of print on 4 June 2008.

Journal of Virology, August 2008, p. 8138-8148, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.00368-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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