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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/41884
Title: Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope
Authors: Alexander Rouvinski
Wanwisa Dejnirattisai
Pablo Guardado-Calvo
Marie Christine Vaney
Arvind Sharma
Stéphane Duquerroy
Piyada Supasa
Wiyada Wongwiwat
Ahmed Haouz
Giovanna Barba-Spaeth
Juthathip Mongkolsapaya
Félix A. Rey
Gavin R. Screaton
Institut Pasteur, Paris
CNRS Centre National de la Recherche Scientifique
Hammersmith Hospital
Universite Paris-Sud XI
Mahidol University
Hebrew University-Hadassah Medical School
Keywords: Biochemistry, Genetics and Molecular Biology;Chemistry
Issue Date: 23-May-2017
Citation: Nature Communications. Vol.8, (2017)
Abstract: © The Author(s) 2017. A problem in the search for an efficient vaccine against dengue virus is the immunodominance of the fusion loop epitope (FLE), a segment of the envelope protein E that is buried at the interface of the E dimers coating mature viral particles. Anti-FLE antibodies are broadly cross-reactive but poorly neutralizing, displaying a strong infection enhancing potential. FLE exposure takes place via dynamic 'breathing' of E dimers at the virion surface. In contrast, antibodies targeting the E dimer epitope (EDE), readily exposed at the E dimer interface over the region of the conserved fusion loop, are very potent and broadly neutralizing. We here engineer E dimers locked by inter-subunit disulfide bonds, and show by X-ray crystallography and by binding to a panel of human antibodies that these engineered dimers do not expose the FLE, while retaining the EDE exposure. These locked dimers are strong immunogen candidates for a next-generation vaccine.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85019563410&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/41884
ISSN: 20411723
Appears in Collections:Scopus 2016-2017

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