2r29
Neutralization of dengue virus by a serotype cross-reactive antibody elucidated by cryoelectron microscopy and x-ray crystallographyNeutralization of dengue virus by a serotype cross-reactive antibody elucidated by cryoelectron microscopy and x-ray crystallography
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins.,Lok SM, Kostyuchenko V, Nybakken GE, Holdaway HA, Battisti AJ, Sukupolvi-Petty S, Sedlak D, Fremont DH, Chipman PR, Roehrig JT, Diamond MS, Kuhn RJ, Rossmann MG Nat Struct Mol Biol. 2008 Mar;15(3):312-7. Epub 2008 Feb 10. PMID:18264114[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- Dengue virus 2 thailand/16681/84
- Mus musculus
- Battisti, A J.
- Chipman, P R.
- Diamond, M S.
- Fremont, D H.
- Holdaway,H A
- Kostyuchenko, V K.
- Kuhn, R J.
- Lok, S M.
- Nybakken, G E.
- Roehrig, J T.
- Rossmann, M G.
- Sedlak,D.
- Sukupolvi-petty,S.
- Atp-binding
- Capsid protein
- Cleavage on pair of basic residue
- Endoplasmic reticulum
- Envelope protein
- Fab-antigen complex
- 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
- Viral protein-immune system complex
- Virion