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Title: Mechanism of enhanced immature dengue virus attachment to endosomal membrane induced by prM antibody
Authors: Wirawan, Melissa
Fibriansah, Guntur
Marzinek, Jan K.
Lim, Xin Xiang
Ng, Thiam-Seng
Sim, Adelene Y. L.
Zhang, Qian
Kostyuchenko, Victor A.
Shi, Jian
Smith, Scott A.
Verma, Chandra Shekhar
Anand, Ganesh
Crowe, James E.
Bond, Peter J.
Lok, Shee-Mei
Keywords: Science::Biological sciences
Issue Date: 2018
Source: Wirawan, M., Fibriansah, G., Marzinek, J. K., Lim, X. X., Ng, T.-S., Sim, A. Y. L., . . . Lok, S-M. (2019). Mechanism of enhanced immature dengue virus attachment to endosomal membrane induced by prM antibody. Structure, 27(2), 253-267. doi:10.1016/j.str.2018.10.009
Journal: Structure
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.
ISSN: 0969-2126
DOI: 10.1016/j.str.2018.10.009
Schools: School of Biological Sciences 
Research Centres: Bioinformatics Institute, A*STAR
Rights: © 2018 Elsevier Ltd. All rights reserved. This paper was published in Structure and is made available with permission of Elsevier Ltd.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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