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Protein Engineering vol. 16 no. 5 pp. 373-379, 2003
© 2003 Oxford University Press

Design and analysis of post-fusion 6-helix bundle of heptad repeat regions from Newcastle disease virus F protein

Jieqing Zhu1, Pengyun Li2, Tinghe Wu1, Feng Gao2, Yi Ding2, Catherine W.-H. Zhang3,4, Zihe Rao2, George F. Gao5,6 and Po Tien1,6

1Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Zhongguancun Beiyitiao, Beijing 100080, 2Laboratory of Structural Biology and MOE Laboratory of Protein Sciences, School of Life Sciences and Bio-Engineering, Tsinghua University, Beijing 100084, China, 3Laboratory of Immunobiology, Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA and 5Nuffield Department of Clinical Medicine, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, UK 4Present address: Oxagen Ltd, Milton Park, Oxfordshire OX14 4RY, UK

6 To whom correspondence should be addressed. e-mail: ggao66{at}yahoo.com; tienpo{at}sun.im.ac.cn

Fusion of paramyxovirus to the cell involves receptor binding of the HN glycoprotein and a number of conformational changes of F glycoprotein. The F protein is expressed as a homotrimer on the virus surface. In the present model, there are at least three conformations of F protein, i.e. native form, pre-hairpin intermediate and the post-fusion state. In the post-fusion state, the two highly conserved heptad repeat (HR) regions of F protein form a stable 6-helix coiled-coil bundle. However, no crystal structure is known for this state for the Newcastle disease virus, although the crystal structure of the F protein native form has been solved recently. Here we deployed an Escherichia coli in vitro expression system to engineer this 6-helix bundle by fusion of either the two HR regions (HR1, linker and HR2) or linking the 6-helix [3 x (HR1, linker and HR2)] together as a single chain. Subsequently, both of them form a stable 6-helix bundle in vitro judging by gel filtration and chemical cross-linking and the proteins show salient features of an {alpha}-helix structure. Crystals diffracting X-rays have been obtained from both protein preparations and the structure determination is under way. This method could be used for crystallization of the post-fusion state HR structures of other viruses.

Received August 13, 2002; revised January 20, 2003; accepted March 13, 2003.


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