8JN5

Cryo-EM structure of dengue virus serotype 3 strain 863DK in complex with human antibody DENV-290 Fab at 37 deg C (subparticle LLR-LRR)

8JN5 の概要

• エントリーDOI: 10.2210/pdb8jn5/pdb
• EMDBエントリー: 36432 36433 36434 36435 36439 36440 36441
• 分子名称: Envelope protein, Membrane protein, Human antibody DENV-290 heavy chain, ... (7 entities in total)
• 機能のキーワード: dengue virus, human antibody, dengue-antibody structure, virus, virus-immune system complex, virus/immune system
• 由来する生物種: Dengue virus type 3; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 215812.42

構造登録者

Fibriansah, G.,Ng, T.S.,Tan, A.W.K.,Shi, J.,Lok, S.M. (登録日: 2023-06-06, 公開日: 2024-06-12, 最終更新日: 2025-12-24)

主引用文献

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

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: 41102151
DOI: 10.1038/s41467-025-64210-7

実験手法

ELECTRON MICROSCOPY (3.6 Å)