ArticleProceedings of the National Academy of Sciences of the United States of America2025
An ultrapotent human antibody neutralizes all maturation states of Zika virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- A distinct E dimer epitope underlies selective recognition by a protective human West Nile virus antibody.EMBO reports · 2026Article
- A review of bloodstream infections-pathogens, pathogenesis, diagnostic strategies, treatment methods-challenges and future aspects.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- Targeting the Zika virus envelope domains I and III as a recombinant vaccine protects mice from lethal challenge.NPJ vaccines · 2026Article
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Authors and funding
11 authors.
Funding
Abstract
Zika virus (ZIKV), a flavivirus, causes a range of clinical complications including microcephaly in human fetuses. Currently, there is no treatment or vaccine. Different maturation states (mature and immature forms) of flavivirus particles have been observed to be released from infected cells and are infectious. To understand how an ultrapotent human antibody (HMAb) A9E can neutralize these Zika particles, we determined the cryoEM structures of the A9E Fab fragment complexed with mature (mZIKV) and immature (immZIKV) ZIKV to 2.8Å and 7.5Å, respectively. A9E binds to an epitope spanning Domain I (EDI), EDIII, and their linker in an E protein protomer in both immZIKV and mZIKV particles. A9E generally inhibited prior to or during virus attachment to cells, via virus aggregation, distortion of virus particles and inhibition of receptor binding. ImmZIKV is particularly sensitive to structural distortion by Fab A9E. The primary mode of infection used by ImmZIKV is via antibody-dependent enhancement of infection (ADE)-the formation of virus complex with nonneutralizing or subneutralizing concentrations of antibodies, that leads to enhanced infection of Fcγ positive myeloid cells. IgG A9E, by itself displays poor ADE activity. When IgG LALA mutant or Fab A9E is added to other enhancing antibody (DV62.5):virus complexes, they can strongly reduce the overall ADE activity. This is likely due to their ability to distort virus particle structure, suggesting that HMAb A9E could be a potential prophylactic and therapeutic candidate against all maturation states of ZIKV.
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