ArticleScientific reports2017
Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- Rational design of flavivirus E protein vaccine optimizes immunogenicity and mitigates antibody dependent enhancement risk.Nature communications · 2025Article
- Design of Hyperglycosylated Zika Virus E Proteins that Focus Antibody Recognition on the Complex E Dimer Epitope.ACS chemical biology · 2025Article
- A two-component cocktail of engineered DIII nanoparticles elicits broadly neutralizing antibody responses against dengue virus in mice.iScience · 2025Article
- Virus-like particle vaccine with authentic quaternary epitopes protects against Zika virus-induced viremia and testicular damage.Journal of virology · 2025Article
- Heterologous prime-boost Zika virus vaccination induces comprehensive humoral and cellular immunity in mouse models.Frontiers in immunology · 2025Article
- Production of Recombinant Zika Virus Envelope Protein by Airlift Bioreactor as a New Subunit Vaccine Platform.International journal of molecular sciences · 2023Article
- Nanobodies Selectively Binding to the Idiotype of a Dengue Virus Neutralizing Antibody Do Not Necessarily Mimic the Viral Epitope.Biomolecules · 2023Article
- Influence of Dosing Regimen and Adjuvant Type on the Immunogenicity of Novel Recombinant Zika Virus-Like Particles.Microbiology spectrum · 2023Article
- The effect of temperature on dengue virus transmission byFrontiers in cellular and infection microbiology · 2023Review
- Review
- Temperate Conditions Limit Zika Virus Genome Replication.Journal of virology · 2022Article
- How Antibodies Recognize Pathogenic Viruses: Structural Correlates of Antibody Neutralization of HIV-1, SARS-CoV-2, and Zika.Viruses · 2021Review
- Designed, highly expressing, thermostable dengue virus 2 envelope protein dimers elicit quaternary epitope antibodies.Science advances · 2021Article
- Effect of ambient temperature on respiratory tract cells exposed to SARS-CoV-2 viral mimicking nanospheres-An experimental study.Biointerphases · 2021Article
- Zika Virus-Like Particles Bearing a Covalent Dimer of Envelope Protein Protect Mice from Lethal Challenge.Journal of virology · 2020Article
- Dimerization of Dengue Virus E Subunits Impacts Antibody Function and Domain Focus.Journal of virology · 2020Article
- Adaptive Immunity to Dengue Virus: Slippery Slope or Solid Ground for Rational Vaccine Design?Pathogens (Basel, Switzerland) · 2020Review
- Oligomeric state of the ZIKV E protein defines protective immune responses.Nature communications · 2019Article
- Characterization of two engineered dimeric Zika virus envelope proteins as immunogens for neutralizing antibody selection and vaccine design.The Journal of biological chemistry · 2019Article
- Therapeutic Fc fusion protein misfolding: A three-phasic cultivation experimental design.PloS one · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dengue and Zika are two of the most important human viral pathogens worldwide. In both cases, the envelope glycoprotein E is the main target of the antibody response. Recently, new complex quaternary epitopes were identified which are the consequence of the arrangement of the antiparallel E dimers on the viral surface. Such epitopes can be exploited to develop more efficient cross-neutralizing vaccines. Here we describe a successful covalent stabilization of E dimers from Dengue and Zika viruses in mammalian cells. Folding and dimerization of secretory E was found to be strongly dependent on temperature but independent of PrM co-expression. In addition, we found that, due to the close relationship between flaviviruses, Dengue and Zika viruses E proteins can form heterodimers and assemble into mosaic viral particles. Finally, we present new virus-free analytical platforms to study and screen antibody responses against Dengue and Zika, which allow for differentiation of epitopes restricted to specific domains, dimers and higher order arrangements of E.
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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.