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• W2617192564 abstract "Abstract 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." @default.
• W2617192564 created "2017-06-05" @default.
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• W2617192564 date "2017-05-23" @default.
• W2617192564 modified "2023-09-30" @default.
• W2617192564 title "Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope" @default.
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• W2617192564 doi "https://doi.org/10.1038/ncomms15411" @default.
• W2617192564 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5457521" @default.
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