期刊
STRUCTURE
卷 26, 期 1, 页码 51-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.11.017
关键词
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资金
- National Natural Science Foundation of China (NSFC) [81501814]
- Anhui Provincial Natural Science Foundation [1508085QH176]
- NSFC-Guangdong Joint Fund [U1132002]
- National Health and Research Council (NHMRC) Australia Fellowship [AF51105]
- NHMRC [1071659, 565526, 1003325, 1110971]
- Australian Research Council (ARC) Linkage [LP120100626]
- National Health and Medical Research Council of Australia [1110971, 1071659] Funding Source: NHMRC
- Australian Research Council [LP120100626] Funding Source: Australian Research Council
Understanding the molecular basis of the neutralizing antibody response to dengue virus (DENV) is an essential component in the design and development of effective vaccines and immunotherapeutics. Here we present the structure of a cross-reactive, neutralizing antibody, 3E31, in complex with domain III (DIII) of the DENV envelope (E) protein and reveal a conserved, temperature-sensitive, cryptic epitope on DIII that is not available in any of the known conformations of E on the dengue virion. We observed that 3E31 inhibits E-mediated membrane fusion, suggesting that the antibody is able to neutralize virus through binding an as-yet uncharacterized intermediate conformation of DENV E and sterically block trimer formation. Finally, we show that, unlike cross-reactive fusion peptide-specific antibodies, 3E31 does not promote antibody-dependent enhancement of infection at sub-neutralizing concentrations. Our results highlight the 3E31 epitope on the E protein DIII as a promising target for immunotherapeutics or vaccine design.
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