9DOF
Octahedral small virus-like particles of dengue virus type 2 (local reconstruction)
Summary for 9DOF
| Entry DOI | 10.2210/pdb9dof/pdb |
| EMDB information | 47082 |
| Descriptor | glycoprotein E, Protein prM (2 entities in total) |
| Functional Keywords | dengue virus type 2, virus, flavivirus, virus-like particle, prm-e protein, fusion protein, cryoem, virus like particle |
| Biological source | dengue virus type 2 More |
| Total number of polymer chains | 6 |
| Total formula weight | 219646.49 |
| Authors | Johnson, A.,Dodes Traian, M.,Walsh, R.M.,Jenni, S.,Harrison, S.C. (deposition date: 2024-09-19, release date: 2024-12-11, Last modification date: 2025-03-12) |
| Primary citation | Johnson, A.,Dodes Traian, M.,Walsh Jr., R.M.,Jenni, S.,Harrison, S.C. Octahedral small virus-like particles of dengue virus type 2. J.Virol., 99:e0180924-e0180924, 2025 Cited by PubMed Abstract: Flavivirus envelope (E) and precursor M (prM) proteins, when ectopically expressed, assemble into empty, virus-like particles (VLPs). Cleavage of prM to M and loss of the pr fragment converts the VLPs from immature to mature particles, mimicking a similar maturation of authentic virions. Most of the VLPs obtained by prM-E expression are smaller than virions; early, low-resolution cryo-EM studies suggested a simple, 60-subunit, icosahedral organization. We describe here the cryo-EM structure of immature, small VLPs (smVLPs) from dengue virus type 2 and show that they have octahedral rather than icosahedral symmetry. The asymmetric unit of the octahedral particle is an asymmetric trimer of prM-E heterodimers, just as it is on icosahedral immature virions; the full, octahedrally symmetric particle thus has 24 such asymmetric trimers or 72 prM-E heterodimers in all. Cleavage of prM and release of pr generates ovoid, somewhat irregular, mature particles. Previous work has shown that mature smVLPs have fusion properties identical to those of virions, consistent with local, virion-like clustering of 36 E dimers on their surface. The cryo-EM structure and the properties of the smVLPs described here relate directly to ongoing efforts to use them as vaccine immunogens. PubMed: 39745459DOI: 10.1128/jvi.01809-24 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.24 Å) |
Structure validation
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