ArticlePLoS pathogens2014
Potent dengue virus neutralization by a therapeutic antibody with low monovalent affinity requires bivalent engagement.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 67 citations in OpenAlex.
- Protective human antibodies against Powassan virus.Journal of virology · 2026Article
- Cryo-ET of IgG bivalent binding on SARS-CoV-2 provides structural basis for antibody avidity.Nature communications · 2026Article
- Hantavirus GnACS infectious diseases · 2025Article
- Optimization of a sarbecovirus llama nanobody-antigen binding interface via a combined computational and phage display protein engineering approach.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The molecular reach of antibodies crucially underpins their viral neutralisation capacity.Nature communications · 2025Article
- Predicting immune response targets in orthoflaviviruses through sequence homology and computational analysis.Journal of molecular modeling · 2024Article
- Antibodies from dengue patients with prior exposure to Japanese encephalitis virus are broadly neutralizing against Zika virus.Communications biology · 2024Article
- Dissecting the contributions of membrane affinity and bivalency of the spider venom protein DkTx to its sustained mode of TRPV1 activation.The Journal of biological chemistry · 2023Article
- prM-reactive antibodies reveal a role for partially mature virions in dengue virus pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dengue virus neutralizing antibody: a review of targets, cross-reactivity, and antibody-dependent enhancement.Frontiers in immunology · 2023Review
- B-cell epitope discovery: The first protein flexibility-based algorithm-Zika virus conserved epitope demonstration.PloS one · 2023Article
- Structural and functional analysis of an inter-Spike bivalent neutralizing antibody against SARS-CoV-2 variants.iScience · 2022Article
- ITS1 amplicon sequencing of feline gut mycobiome of Malaysian local breeds using Nanopore Flongle.Archives of microbiology · 2022Article
- Charged Residue Implantation Improves the Affinity of a Cross-Reactive Dengue Virus Antibody.International journal of molecular sciences · 2022Article
- Stochastic modeling of antibody binding predicts programmable migration on antigen patterns.Nature computational science · 2022Article
- Discovery of B-cell epitopes for development of dengue vaccines and antibody therapeutics.Medical microbiology and immunology · 2022Review
- Flavivirus Entry Inhibitors.Advances in experimental medicine and biology · 2022Article
- Prevalence of arbovirus antibodies in young healthy adult population in Brazil.Parasites & vectors · 2021Article
- Article
- Diverse contributions of avidity to the broad neutralization of Dengue virus by antibodies targeting the E dimer epitope.Virology · 2021Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
Abstract
We recently described our most potently neutralizing monoclonal antibody, E106, which protected against lethal Dengue virus type 1 (DENV-1) infection in mice. To further understand its functional properties, we determined the crystal structure of E106 Fab in complex with domain III (DIII) of DENV-1 envelope (E) protein to 2.45 Å resolution. Analysis of the complex revealed a small antibody-antigen interface with the epitope on DIII composed of nine residues along the lateral ridge and A-strand regions. Despite strong virus neutralizing activity of E106 IgG at picomolar concentrations, E106 Fab exhibited a ∼20,000-fold decrease in virus neutralization and bound isolated DIII, E, or viral particles with only a micromolar monovalent affinity. In comparison, E106 IgG bound DENV-1 virions with nanomolar avidity. The E106 epitope appears readily accessible on virions, as neutralization was largely temperature-independent. Collectively, our data suggest that E106 neutralizes DENV-1 infection through bivalent engagement of adjacent DIII subunits on a single virion. The isolation of anti-flavivirus antibodies that require bivalent binding to inhibit infection efficiently may be a rare event due to the unique icosahedral arrangement of envelope proteins on the virion surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.