Unknown

Dataset Information

0

Structures of immature flavivirus particles.


ABSTRACT: Structures of prM-containing dengue and yellow fever virus particles were determined to 16 and 25 A 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.

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC156766 | biostudies-literature | 2003 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications


Structures of prM-containing dengue and yellow fever virus particles were determined to 16 and 25 A 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 th  ...[more]

Similar Datasets

| S-EPMC8121421 | biostudies-literature
| S-EPMC5730767 | biostudies-literature
| S-EPMC4635454 | biostudies-literature
| S-EPMC5707545 | biostudies-literature
| EMPIAR-11387 | biostudies-other
| EMPIAR-10776 | biostudies-other
| S-EPMC8880525 | biostudies-literature
| S-EPMC10902078 | biostudies-literature
| S-EPMC5906032 | biostudies-literature
| S-EPMC7177695 | biostudies-literature