Journal article
Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
- Abstract:
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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 viru...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 6.7MB)
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- Publisher copy:
- 10.1038/s41598-017-01097-5
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Authors
Funding
+ International Centre for Genetic Engineering and Biotechnology
More from this funder
Funding agency for:
Slon Campos, J
Bibliographic Details
- Publisher:
- Nature Publishing Group Publisher's website
- Journal:
- Scientific reports Journal website
- Volume:
- 7
- Issue:
- 1
- Pages:
- 14
- Publication date:
- 2017-04-19
- Acceptance date:
- 2017-03-24
- DOI:
- EISSN:
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2045-2322
- Pmid:
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28424472
- Source identifiers:
-
863434
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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pubs:863434
- UUID:
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uuid:5b1c7065-65f8-4d9a-81e8-8f0067c9492a
- Local pid:
- pubs:863434
- Deposit date:
- 2018-07-05
Terms of use
- Copyright holder:
- J L Slon Campos et al
- Copyright date:
- 2017
- Notes:
-
© The Author(s) 2017. This article is licensed under a Creative Commons Attribution 4.0 International
License, which permits use, sharing, adaptation, distribution and reproduction in any medium or
format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative
Commons license, and indicate if changes were made.
- Licence:
- CC Attribution (CC BY)
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