ArticleThe Journal of biological chemistry2018
Physiological temperatures reduce dimerization of dengue and Zika virus recombinant envelope proteins.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Detection of dengue virus serotype 2 in local Aedes aegypti populations, Madeira Island, Portugal, 2025.Parasites & vectors · 2026Article
- Multivalent administration of dengue E dimers on liposomes elicits type-specific neutralizing responses without immune interference.NPJ vaccines · 2025Article
- Stabilized dengue virus 2 envelope subunit vaccine redirects the neutralizing antibody response to all E-domains.Journal of virology · 2025Article
- Heterologous prime-boost Zika virus vaccination induces comprehensive humoral and cellular immunity in mouse models.Frontiers in immunology · 2025Article
- 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
- The ganglioside GM1a functions as a coreceptor/attachment factor for dengue virus during infection.The Journal of biological chemistry · 2022Article
- Stabilizing proteins, simplified: A Rosetta-based webtool for predicting favorable mutations.Protein science : a publication of the Protein Society · 2022Article
- Temperate Conditions Limit Zika Virus Genome Replication.Journal of virology · 2022Article
- Designed, highly expressing, thermostable dengue virus 2 envelope protein dimers elicit quaternary epitope antibodies.Science advances · 2021Article
- Human plasmacytoid dendritic cells at the crossroad of type I interferon-regulated B cell differentiation and antiviral response to tick-borne encephalitis virus.PLoS pathogens · 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
- Identification of Dengue Virus Serotype 3 Specific Antigenic Sites Targeted by Neutralizing Human Antibodies.Cell host & microbe · 2020Article
- Impact of temperature on the extrinsic incubation period of Zika virus in Aedes aegypti.PLoS neglected tropical diseases · 2020Article
- Nanoparticle delivery of a tetravalent E protein subunit vaccine induces balanced, type-specific neutralizing antibodies to each dengue virus serotype.PLoS neglected tropical diseases · 2018Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
The spread of dengue (DENV) and Zika virus (ZIKV) is a major public health concern. The primary target of antibodies that neutralize DENV and ZIKV is the envelope (E) glycoprotein, and there is interest in using soluble recombinant E (sRecE) proteins as subunit vaccines. However, the most potent neutralizing antibodies against DENV and ZIKV recognize epitopes on the virion surface that span two or more E proteins. Therefore, to create effective DENV and ZIKV vaccines, presentation of these quaternary epitopes may be necessary. The sRecE proteins from DENV and ZIKV crystallize as native-like dimers, but studies in solution suggest that these dimers are marginally stable. To better understand the challenges associated with creating stable sRecE dimers, we characterized the thermostability of sRecE proteins from ZIKV and three DENV serotypes, DENV2-4. All four proteins irreversibly unfolded at moderate temperatures (46-53 °C). At 23 °C and low micromolar concentrations, DENV2 and ZIKV were primarily dimeric, and DENV3-4 were primarily monomeric, whereas at 37 °C, all four proteins were predominantly monomeric. We further show that the dissociation constant for DENV2 dimerization is very temperature-sensitive, ranging from <1 μm at 25 °C to 50 μm at 41 °C, due to a large exothermic enthalpy of binding of -79 kcal/mol. We also found that quaternary epitope antibody binding to DENV2-4 and ZIKV sRecE is reduced at 37 °C. Our observation of reduced sRecE dimerization at physiological temperature highlights the need for stabilizing the dimer as part of its development as a subunit vaccine.
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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.