3J8D

Cryoelectron microscopy of dengue-Fab E104 complex at pH 5.5

Summary for 3J8D

• Entry DOI: 10.2210/pdb3j8d/pdb
• EMDB information: 6146
• Descriptor: glycoprotein DIII, antibody E111 Fab fragment, Envelope protein E (3 entities in total)
• Functional Keywords: dengue virus, denv2 fab e104, low ph, fusion trimer, virus-immune system complex, virus/immune system
• Biological source: Dengue virus 2 Thailand/16681/84 (DENV-2); More
• Total number of polymer chains: 7
• Total formula weight: 245965.82

Authors

Zhang, X.Z.,Sheng, J.,Austin, S.K.,Hoornweg, T.,Smit, J.M.,Kuhn, R.J.,Diamond, M.S.,Rossmann, M.G. (deposition date: 2014-10-13, release date: 2014-11-12, Last modification date: 2024-02-21)

Primary citation

Zhang, X.,Sheng, J.,Austin, S.K.,Hoornweg, T.E.,Smit, J.M.,Kuhn, R.J.,Diamond, M.S.,Rossmann, M.G.
Structure of Acidic pH Dengue Virus Showing the Fusogenic Glycoprotein Trimers.
J.Virol., 89:743-750, 2015

PubMed Abstract: Flaviviruses undergo large conformational changes during their life cycle. Under acidic pH conditions, the mature virus forms transient fusogenic trimers of E glycoproteins that engage the lipid membrane in host cells to initiate viral fusion and nucleocapsid penetration into the cytoplasm. However, the dynamic nature of the fusogenic trimer has made the determination of its structure a challenge. Here we have used Fab fragments of the neutralizing antibody DV2-E104 to stop the conformational change of dengue virus at an intermediate stage of the fusion process. Using cryo-electron microscopy, we show that in this intermediate stage, the E glycoproteins form 60 trimers that are similar to the predicted "open" fusogenic trimer.

PubMed: 25355881
DOI: 10.1128/JVI.02411-14

Experimental method

ELECTRON MICROSCOPY (26 Å)