Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms14339
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dc.titleConformational changes in intact dengue virus reveal serotype-specific expansion
dc.contributor.authorLim, X.-X
dc.contributor.authorChandramohan, A
dc.contributor.authorLim, X.Y.E
dc.contributor.authorBag, N
dc.contributor.authorSharma, K.K
dc.contributor.authorWirawan, M
dc.contributor.authorWohland, T
dc.contributor.authorLok, S.-M
dc.contributor.authorAnand, G.S
dc.date.accessioned2020-09-04T03:42:08Z
dc.date.available2020-09-04T03:42:08Z
dc.date.issued2017
dc.identifier.citationLim, 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
dc.identifier.issn2041-1723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/174432
dc.description.abstractDengue 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.
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectamide
dc.subjectepitope
dc.subjectstructural protein
dc.subjectviral protein
dc.subjectvirus antibody
dc.subjectvirus envelope protein
dc.subjectantibody
dc.subjectdengue fever
dc.subjectdeuterium
dc.subjectenergy flow
dc.subjecthomology
dc.subjecthost
dc.subjecthydrogen
dc.subjectmass spectrometry
dc.subjectvirus
dc.subjectArticle
dc.subjectconformational transition
dc.subjectcontrolled study
dc.subjectDengue virus
dc.subjectDengue virus 1
dc.subjectDengue virus 2
dc.subjectdeuterium hydrogen exchange
dc.subjectdynamics
dc.subjectepitope mapping
dc.subjectfluorescence resonance energy transfer
dc.subjectgene locus
dc.subjectmass spectrometry
dc.subjectnonhuman
dc.subjectserotype
dc.subjecttemperature dependence
dc.subjectvirus particle
dc.subjectvirus strain
dc.subjectamino acid sequence
dc.subjectchemistry
dc.subjectconformation
dc.subjectdengue
dc.subjectDengue virus
dc.subjectgenetics
dc.subjecthost pathogen interaction
dc.subjecthuman
dc.subjectimmunology
dc.subjectmetabolism
dc.subjectmolecular model
dc.subjectphysiology
dc.subjectprotein conformation
dc.subjectserotype
dc.subjecttemperature
dc.subjectvirion
dc.subjectvirology
dc.subjectDengue virus
dc.subjectAmino Acid Sequence
dc.subjectAntibodies, Viral
dc.subjectDengue
dc.subjectDengue Virus
dc.subjectDeuterium Exchange Measurement
dc.subjectHost-Pathogen Interactions
dc.subjectHumans
dc.subjectModels, Molecular
dc.subjectMolecular Conformation
dc.subjectProtein Conformation
dc.subjectSerogroup
dc.subjectTemperature
dc.subjectViral Envelope Proteins
dc.subjectVirion
dc.typeArticle
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.contributor.departmentBIOLOGY (NU)
dc.contributor.departmentDUKE-NUS MEDICAL SCHOOL
dc.description.doi10.1038/ncomms14339
dc.description.sourcetitleNature Communications
dc.description.volume8
dc.description.page14339
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