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TitleStructural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody.
Journal, issue, pagesEMBO J, Vol. 28, Issue 20, Page 3269-3276, Year 2009
Publish dateOct 21, 2009
AuthorsMickaël V Cherrier / Bärbel Kaufmann / Grant E Nybakken / Shee-Mei Lok / Julia T Warren / Beverly R Chen / Christopher A Nelson / Victor A Kostyuchenko / Heather A Holdaway / Paul R Chipman / Richard J Kuhn / Michael S Diamond / Michael G Rossmann / Daved H Fremont /
PubMed AbstractFlaviviruses are a group of human pathogens causing severe encephalitic or hemorrhagic diseases that include West Nile, dengue and yellow fever viruses. Here, using X-ray crystallography we have ...Flaviviruses are a group of human pathogens causing severe encephalitic or hemorrhagic diseases that include West Nile, dengue and yellow fever viruses. Here, using X-ray crystallography we have defined the structure of the flavivirus cross-reactive antibody E53 that engages the highly conserved fusion loop of the West Nile virus envelope glycoprotein. Using cryo-electron microscopy, we also determined that E53 Fab binds preferentially to spikes in noninfectious, immature flavivirions but is unable to bind significantly to mature virions, consistent with the limited solvent exposure of the epitope. We conclude that the neutralizing impact of E53 and likely similar fusion-loop-specific antibodies depends on its binding to the frequently observed immature component of flavivirus particles. Our results elucidate how fusion-loop antibodies, which comprise a significant fraction of the humoral response against flaviviruses, can function to control infection without appreciably recognizing mature virions. As these highly cross-reactive antibodies are often weakly neutralizing they also may contribute to antibody-dependent enhancement and flavi virus pathogenesis thereby complicating development of safe and effective vaccines.
External linksEMBO J / PubMed:19713934 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3 - 23.0 Å
Structure data

5102

3ixy

EMDB-5102: Immature Dengue Virus (DENV) in complex with Fab fragments of the anti-fusion loop antibody E53
PDB-3ixy: The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53
Method: EM (single particle) / Resolution: 23.0 Å

5103

3ixx

EMDB-5103: Immature West Nile Virus (WNV) in complex with Fab fragments of the anti-fusion loop antibody E53
PDB-3ixx: The pseudo-atomic structure of West Nile immature virus in complex with Fab fragments of the anti-fusion loop antibody E53
Method: EM (single particle) / Resolution: 15.0 Å

PDB-3i50:
Crystal structure of the West Nile Virus envelope glycoprotein in complex with the E53 antibody Fab
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Source
  • west nile virus
  • mus musculus (house mouse)
  • dengue virus 2
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / ANTIBODY / FAB / VIRUS / ENVELOPE / IMMUNOGLOBULIN / FUSION LOOP / Disulfide bond / Envelope protein / Membrane / Transmembrane / Virion / VIRAL PROTEIN-IMMUNE SYSTEM complex / West Nile Virus / WNV / immature / E53 / ATP-binding / Helicase / Hydrolase / Nucleotide-binding / RNA replication / Icosahedral virus / Dengue Virus / DENV / Capsid protein / Cleavage on pair of basic residues / Core protein / Endoplasmic reticulum / Glycoprotein / Secreted

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