Biochemical and biophysical analysis of heptad repeat regions from the fusion protein of Menangle virus,a newly emergent paramyxovirus |
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| Authors: | J. Q. Zhu C. W.-H. Zhang Z. Rao P. Tien G. F. Gao |
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| Affiliation: | (1) Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China, CN;(2) Oxagen Ltd., Milton Park, Oxfordshire, U.K., GB;(3) Laboratory of Structural Biology and MOE Laboratory of Protein Sciences, School of Life Sciences and Bio-Engineering, Tsinghua University, Beijing, China, CN;(4) Nuffield Department of Clinical Medicine, John Radcliffe Hospital, University of Oxford, Oxford, U.K., GB |
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| Abstract: | ![]()
E. coli in vitro expression system. The GST-removed purified 2-Helix protein could form a stable trimer in vitro judging by gel-filtration and chemical cross-linking. CD spectra showed that the 2-Helix protein had a high percentage of α-helix and was very thermo-stable. Crystals of the 2-Helix protein preparations have been obtained in many conditions with hanging-drop diffusion method. These results indicated that Menangle virus has the common features of the fusion protein for other paramyxoviruses and should adopt a similar fusion mechanism to other members. As the HR regions of Menangle virus F protein could form stable six-helix bundle coiled coil structure, they should be used as drug target for the design of fusion inhibitors, as successfully used for other parmyxoviruses. This is especially relevant to such a newly emergent virus with zoonotic potentials. Received January 23, 2003; accepted February 28, 2003 Published online April 28, 2003 |
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