Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion

Richard J. Kuhn, Wei Zhang, Michael G. Rossmann, Sergei V. Pletnev, Jeroen Corver, Edith Lenches, Christopher T. Jones, Suchetana Mukhopadhyay, Paul R. Chipman, Ellen G. Strauss, Timothy S. Baker, James H. Strauss

Research output: Contribution to journalArticlepeer-review

1262 Scopus citations


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 β barrels of domain II of the glycoprotein E are inserted into the cellular membrane.

Original languageEnglish (US)
Pages (from-to)717-725
Number of pages9
Issue number5
StatePublished - Mar 8 2002
Externally publishedYes

Bibliographical note

Funding Information:
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).


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