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TitleBinding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins.
Journal, issue, pagesNat Struct Mol Biol, Vol. 15, Issue 3, Page 312-317, Year 2008
Publish dateFeb 10, 2008
AuthorsShee-Mei Lok / Victor Kostyuchenko / Grant E Nybakken / Heather A Holdaway / Anthony J Battisti / Soila Sukupolvi-Petty / Dagmar Sedlak / Daved H Fremont / Paul R Chipman / John T Roehrig / Michael S Diamond / Richard J Kuhn / Michael G Rossmann /
PubMed AbstractThe monoclonal antibody 1A1D-2 has been shown to strongly neutralize dengue virus serotypes 1, 2 and 3, primarily by inhibiting attachment to host cells. A crystal structure of its antigen binding ...The monoclonal antibody 1A1D-2 has been shown to strongly neutralize dengue virus serotypes 1, 2 and 3, primarily by inhibiting attachment to host cells. A crystal structure of its antigen binding fragment (Fab) complexed with domain III of the viral envelope glycoprotein, E, showed that the epitope would be partially occluded in the known structure of the mature dengue virus. Nevertheless, antibody could bind to the virus at 37 degrees C, suggesting that the virus is in dynamic motion making hidden epitopes briefly available. A cryo-electron microscope image reconstruction of the virus:Fab complex showed large changes in the organization of the E protein that exposed the epitopes on two of the three E molecules in each of the 60 icosahedral asymmetric units of the virus. The changes in the structure of the viral surface are presumably responsible for inhibiting attachment to cells.
External linksNat Struct Mol Biol / PubMed:18264114
MethodsEM (single particle) / X-ray diffraction
Resolution3 - 24.0 Å
Structure data

1418

2r6p

EMDB-1418: Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins
PDB-2r6p: Fit of E protein and Fab 1A1D-2 into 24 angstrom resolution cryoEM map of Fab complexed with dengue 2 virus.
Method: EM (single particle) / Resolution: 24.0 Å

PDB-2r29:
Neutralization of dengue virus by a serotype cross-reactive antibody elucidated by cryoelectron microscopy and x-ray crystallography
Method: X-RAY DIFFRACTION / Resolution: 3.0 Å

PDB-2r69:
Crystal structure of Fab 1A1D-2 complexed with E-DIII of Dengue virus at 3.8 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 3.8 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • mus musculus (house mouse)
  • dengue virus 2 thailand/16681/84
  • dengue virus 2 puerto rico/pr159-s1/1969
KeywordsViral protein/Immune system / Fab-antigen complex / ATP-binding / Capsid protein / Cleavage on pair of basic residues / Endoplasmic reticulum / Envelope protein / Glycoprotein / Helicase / Hydrolase / Membrane / Metal-binding / Multifunctional enzyme / Nucleotide-binding / Nucleotidyltransferase / Nucleus / Phosphorylation / Protease / Ribonucleoprotein / RNA replication / RNA-binding / RNA-directed RNA polymerase / Secreted / Serine protease / Transcription / Transcription regulation / Transferase / Transmembrane / Viral nucleoprotein / Virion / Viral protein-Immune system COMPLEX / Core protein / Virus/Immune System / Fab / dengue / virus / neutralization / Virus-Immune System COMPLEX / icosahedral virus

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