Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
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 o...
| Main Authors: | , , , , , , |
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| Formato: | Journal article |
| Idioma: | English |
| Publicado em: |
Nature Publishing Group
2017
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| _version_ | 1826274191093006336 |
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| author | Slon Campos, J Marchese, S Rana, J Mossenta, M Poggianella, M Bestagno, M Burrone, O |
| author_facet | Slon Campos, J Marchese, S Rana, J Mossenta, M Poggianella, M Bestagno, M Burrone, O |
| author_sort | Slon Campos, J |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T22:39:41Z |
| format | Journal article |
| id | oxford-uuid:5b1c7065-65f8-4d9a-81e8-8f0067c9492a |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:39:41Z |
| publishDate | 2017 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | oxford-uuid:5b1c7065-65f8-4d9a-81e8-8f0067c9492a2022-03-26T17:20:08ZTemperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cellsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5b1c7065-65f8-4d9a-81e8-8f0067c9492aEnglishSymplectic Elements at OxfordNature Publishing Group2017Slon Campos, JMarchese, SRana, JMossenta, MPoggianella, MBestagno, MBurrone, ODengue 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. |
| spellingShingle | Slon Campos, J Marchese, S Rana, J Mossenta, M Poggianella, M Bestagno, M Burrone, O Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells |
| title | Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells |
| title_full | Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells |
| title_fullStr | Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells |
| title_full_unstemmed | Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells |
| title_short | Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells |
| title_sort | temperature dependent folding allows stable dimerization of secretory and virus associated e proteins of dengue and zika viruses in mammalian cells |
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