Structures of immature flavivirus particles

Ying Zhang, Jeroen Corver, Paul R. Chipman, Wei Zhang, Sergei V. Pletnev, Dagmar Sedlak, Timothy S. Baker, James H. Strauss, Richard J. Kuhn, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

384 Scopus citations


Structures of prM-containing dengue and yellow fever virus particles were determined to 16 and 25 Å resolution, respectively, by cryoelectron microscopy and image reconstruction techniques. The closely similar structures show 60 icosahedrally organized trimeric spikes on the particle surface. Each spike consists of three prM:E heterodimers, where E is an envelope glycoprotein and prM is the precursor to the membrane protein M. The pre-peptide components of the prM proteins in each spike cover the fusion peptides at the distal ends of the E glycoproteins in a manner similar to the organization of the glycoproteins in the alphavirus spikes. Each heterodimer is associated with an E and a prM transmembrane density. These transmembrane densities represent either an EE or prMprM antiparallel coiled coil by which each protein spans the membrane twice, leaving the C-terminus of each protein on the exterior of the viral membrane, consistent with the predicted membrane-spanning domains of the unprocessed polyprotein.

Original languageEnglish (US)
Pages (from-to)2604-2613
Number of pages10
JournalEMBO Journal
Issue number11
StatePublished - Jun 2 2003


  • Conformational changes
  • Dengue virus
  • EM reconstruction
  • Immature particles


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