Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms14339
Title: Conformational changes in intact dengue virus reveal serotype-specific expansion
Authors: Lim, X.-X 
Chandramohan, A 
Lim, X.Y.E
Bag, N 
Sharma, K.K 
Wirawan, M
Wohland, T 
Lok, S.-M 
Anand, G.S 
Keywords: amide
epitope
structural protein
viral protein
virus antibody
virus envelope protein
antibody
dengue fever
deuterium
energy flow
homology
host
hydrogen
mass spectrometry
virus
Article
conformational transition
controlled study
Dengue virus
Dengue virus 1
Dengue virus 2
deuterium hydrogen exchange
dynamics
epitope mapping
fluorescence resonance energy transfer
gene locus
mass spectrometry
nonhuman
serotype
temperature dependence
virus particle
virus strain
amino acid sequence
chemistry
conformation
dengue
Dengue virus
genetics
host pathogen interaction
human
immunology
metabolism
molecular model
physiology
protein conformation
serotype
temperature
virion
virology
Dengue virus
Amino Acid Sequence
Antibodies, Viral
Dengue
Dengue Virus
Deuterium Exchange Measurement
Host-Pathogen Interactions
Humans
Models, Molecular
Molecular Conformation
Protein Conformation
Serogroup
Temperature
Viral Envelope Proteins
Virion
Issue Date: 2017
Publisher: Nature Publishing Group
Citation: Lim, X.-X, Chandramohan, A, Lim, X.Y.E, Bag, N, Sharma, K.K, Wirawan, M, Wohland, T, Lok, S.-M, Anand, G.S (2017). Conformational changes in intact dengue virus reveal serotype-specific expansion. Nature Communications 8 : 14339. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms14339
Abstract: Dengue virus serotype 2 (DENV2) alone undergoes structural expansion at 37 °C (associated with host entry), despite high sequence and structural homology among the four known serotypes. The basis for this differential expansion across strains and serotypes is unknown and necessitates mapping of the dynamics of dengue whole viral particles to describe their coordinated motions and conformational changes when exposed to host-like environments. Here we capture the dynamics of intact viral particles of two serotypes, DENV1 and DENV2, by amide hydrogen/deuterium exchange mass spectrometry (HDXMS) and time resolved Förster Resonance Energy Transfer. Our results show temperature-dependent dynamics hotspots on DENV2 and DENV1 particles with DENV1 showing expansion at 40 °C but not at 37 °C. HDXMS measurement of virion dynamics in solution offers a powerful approach to identify potential epitopes, map virus-antibody complex structure and dynamics, and test effects of multiple host-specific perturbations on viruses and virus-antibody complexes. © The Author(s) 2017.
Source Title: Nature Communications
URI: https://scholarbank.nus.edu.sg/handle/10635/174432
ISSN: 2041-1723
DOI: 10.1038/ncomms14339
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