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Published 2003 | Supplemental Material
Journal Article Open

Structures of immature flavivirus particles

Abstract

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.

Additional Information

© European Molecular Biology Organization. Received January 29, 2003; revised April 4, 2003; accepted April 9, 2003. We thank Suchetana (Tuli) Mukhopadhyay and Ellen Strauss for many helpful discussions, Rob Ashmore, Chuan (River) Xiao, Yongchang Ji and Dan Marinescu for the use of their various computer programs that were essential for calculating the image reconstruction of the prM particles, and Cheryl Towell and Sharon Wilder for help in preparing the manuscript. We are grateful for an equipment grant from the Keck Foundation that provided the CM300 electron microscope. The work was supported by an NIH Project Program Grant (AI 45976) to M.G.R., R.J.K. and T.S.B., NIH grants to T.S.B. (GM33050) and J.H.S. (AI 10793) and an NSF grant to T.S.B. (DBI 9986316).

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August 19, 2023
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