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Published March 8, 2002 | Accepted Version
Journal Article Open

Structure of Dengue Virus: Implications for Flavivirus Organization, Maturation, and Fusion


The first structure of a flavivirus has been determined by using a combination of cryoelectron microscopy and fitting of the known structure of glycoprotein E into the electron density map. The virus core, within a lipid bilayer, has a less-ordered structure than the external, icosahedral scaffold of 90 glycoprotein E dimers. The three E monomers per icosahedral asymmetric unit do not have quasiequivalent symmetric environments. Difference maps indicate the location of the small membrane protein M relative to the overlaying scaffold of E dimers. The structure suggests that flaviviruses, and by analogy also alphaviruses, employ a fusion mechanism in which the distal barrels of domain II of the glycoprotein E are inserted into the cellular membrane.

Additional Information

© 2002 Cell Press. Received: October 3, 2001. Revised: December 21, 2001. We thank Sharon Wilder for help in preparation of the manuscript. The work was supported by a National Institutes of Health Program Project Grant to M.G.R., R.J.K., and T.S.B. (AI45976), grant AI20612 to J.H.S., grant AI10793 to J.H.S. and E.G.S., and a Purdue University redevelopment award. C.T.J. is a recipient of a National Institutes of Health biophysics training grant (GM08296). Accession Numbers: The coordinates for dengue virus have been deposited in the Protein Data Bank with the accession number 1K4R.

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