8JN2
Cryo-EM structure of dengue virus serotype 3 strain 863DK in complex with human antibody DENV-115 Fab at 4 deg C (subparticle LLR-LRR)
Summary for 8JN2
| Entry DOI | 10.2210/pdb8jn2/pdb |
| EMDB information | 36429 36430 36431 36436 36437 36438 |
| Descriptor | Envelope protein, Membrane protein, Human antibody DENV-115 heavy chain, ... (6 entities in total) |
| Functional Keywords | dengue virus, human antibody, dengue-antibody structure, virus, virus-immune system complex, virus/immune system |
| Biological source | Dengue virus type 3 More |
| Total number of polymer chains | 8 |
| Total formula weight | 214389.84 |
| Authors | Fibriansah, G.,Ng, T.S.,Tan, A.W.K.,Shi, J.,Lok, S.M. (deposition date: 2023-06-06, release date: 2024-06-12, Last modification date: 2025-12-24) |
| Primary citation | Fibriansah, G.,Ng, T.S.,Lim, X.N.,Shebanova, A.,Ng, L.C.,Tan, S.L.,Tan, A.W.K.,Shi, J.,Crowe Jr., J.E.,Lok, S.M. Ultrapotent human antibodies lock E protein dimers central region of diverse DENV3 morphological variants. Nat Commun, 16:9182-9182, 2025 Cited by PubMed Abstract: Dengue virus (DENV) consists of four serotypes (DENV1-4). Current vaccines induce differing levels of immune response against the four serotypes, that might prime recipients to develop severe disease in subsequent infections. Several DENV tetravalent vaccine clinical trials suggested an increased incidence in severe DENV3 cases, suggesting a need to develop DENV3 therapeutics. Human monoclonal antibodies (HMAbs) DENV-290 and DENV-115 are ultrapotent against diverse DENV3 strains with differing particle morphologies. They mainly neutralize by inhibition of virus attachment to cells. CryoEM structures of Fabs complexed with differing DENV3 morphological variants show their Fabs binding across two E protein protomers at the center of the E dimer. This new class of E protein dimer binding antibodies is named EDE-C. The cryoEM structures also show how IgGs engage the DENV particles. Results define the structural and molecular basis for the ultrapotent activity of EDE-C antibodies. PubMed: 41102151DOI: 10.1038/s41467-025-64210-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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