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6IDL

Cryo-EM structure of Immature Dengue virus serotype 3 in complex with human antibody 1H10 Fab at pH 5.0 (Class II particle)

Summary for 6IDL
Entry DOI10.2210/pdb6idl/pdb
EMDB information9649 9650 9651
DescriptorEnvelope protein, Premembrane protein, Fab 1H10 heavy chain (V-region), ... (4 entities in total)
Functional Keywordsimmature dengue virus, human antibody, virus
Biological sourceDengue virus 3
More
Total number of polymer chains9
Total formula weight253323.49
Authors
Wirawan, M.,Fibriansah, G.,Ng, T.S.,Zhang, Q.,Kostyuchenko, V.A.,Shi, J.,Lok, S.M. (deposition date: 2018-09-10, release date: 2018-12-12, Last modification date: 2024-03-27)
Primary citationWirawan, M.,Fibriansah, G.,Marzinek, J.K.,Lim, X.X.,Ng, T.S.,Sim, A.Y.L.,Zhang, Q.,Kostyuchenko, V.A.,Shi, J.,Smith, S.A.,Verma, C.S.,Anand, G.,Crowe Jr., J.E.,Bond, P.J.,Lok, S.M.
Mechanism of Enhanced Immature Dengue Virus Attachment to Endosomal Membrane Induced by prM Antibody.
Structure, 27:253-267.e8, 2019
Cited by
PubMed Abstract: Dengue virus (DENV) particles are released from cells in different maturation states. Fully immature DENV (immDENV) is generally non-infectious, but can become infectious when complexed with anti-precursor membrane (prM) protein antibodies. It is unknown how anti-prM antibody-coated particles can undergo membrane fusion since the prM caps the envelope (E) protein fusion loop. Here, we determined cryoelectron microscopy (cryo-EM) maps of the immDENV:anti-prM complex at different pH values, mimicking the extracellular (pH 8.0) or endosomal (pH 5.0) environments. At pH 5.0, there are two structural classes with fewer antibodies bound than at pH 8.0. These classes may represent different maturation states. Molecular simulations, together with the measured high-affinity pr:antibody interaction (versus the weak pr:E interaction) and also the low pH cryo-EM structures, suggest how antibody:pr complex can dislodge from the E protein at low pH. This exposes the E protein fusion loop enhancing virus interaction with endosomes.
PubMed: 30471923
DOI: 10.1016/j.str.2018.10.009
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (25 Å)
Structure validation

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