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Related Experiment Video

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A Simple Flow Cytometry Based Assay to Determine In Vitro Antibody Dependent Enhancement of Dengue Virus Using Zika Virus Convalescent Serum
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Antibody affinity versus dengue morphology influences neutralization.

Guntur Fibriansah1,2, Elisa X Y Lim1,2, Jan K Marzinek3

  • 1Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, Singapore.

Plos Pathogens
|February 23, 2021
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Summary

This study reveals how dengue virus (DENV) surface structure affects antibody neutralization. A specific antibody effectively neutralizes DENV1 but is less effective against DENV2, highlighting the need for high-affinity antibodies targeting diverse DENV morphologies.

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Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Dengue virus (DENV) serotypes 1-4 exhibit diverse surface morphologies.
  • These morphological differences influence antigenic properties and antibody interactions at body temperature.

Purpose of the Study:

  • To investigate the neutralizing efficacy of a cross-reactive human monoclonal antibody (HMAb) 1C19 against DENV1 and DENV2 strains with varying morphologies.
  • To characterize the binding epitope and mechanism of action of HMAb 1C19.

Main Methods:

  • Hydrogen deuterium exchange mass spectrometry (HDX-MS)
  • Cryo-electron microscopy (cryo-EM)
  • Molecular dynamics (MD) simulations
  • Binding affinity assays
  • Neutralization assays

Main Results:

  • The HMAb 1C19 epitope was mapped to E protein domain II, identified as partially hidden on the virus surface.
  • HMAb 1C19 demonstrated high binding affinity and potent neutralization of all tested DENV1 strains, irrespective of morphology.
  • Neutralization of DENV2 strains by HMAb 1C19 was dependent on epitope exposure on bumpy-surfaced particles, with lower overall efficacy compared to DENV1.

Conclusions:

  • Antibody affinity and epitope accessibility are critical factors in neutralizing diverse DENV morphologies.
  • HMAb 1C19's differential activity underscores the challenge of developing broad-spectrum dengue therapeutics.
  • Selecting high-affinity antibodies capable of neutralizing various DENV forms is crucial for effective therapeutic strategies.