期刊
CELL REPORTS
卷 25, 期 13, 页码 3750-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2018.12.001
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资金
- Medical Research Council [MR/L009528/1, MR/K024426/1, MR/N002091/1]
- Wellcome [089026/Z/09/Z]
- European Research Council [614725-PATHPHYLODYN]
- European Research Council under the European Union [649053]
- Oak Foundation Fellowship
- PHE PhD studentship
- [203141/Z/16/Z]
- MRC [MC_PC_15068, MR/K024426/1, MR/N002091/1, MR/L009528/1, MC_UU_12014/8] Funding Source: UKRI
- Wellcome Trust [089026/Z/09/Z] Funding Source: Wellcome Trust
- European Research Council (ERC) [649053] Funding Source: European Research Council (ERC)
The Gn subcomponent of the Gn-Gc assembly that envelopes the human and animal pathogen, Rift Valley fever virus (RVFV), is a primary target of the neutralizing antibody response. To better understand the molecular basis for immune recognition, we raised a class of neutralizing monoclonal antibodies (nAbs) against RVFV Gn, which exhibited protective efficacy in a mouse infection model. Structural characterization revealed that these nAbs were directed to the membrane-distal domain of RVFVGn and likely prevented virus entry into a host cell by blocking fusogenic rearrangements of the Gn-Gc lattice. Genome sequence analysis confirmed that this region of the RVFV Gn-Gc assembly was under selective pressure and constituted a site of vulnerability on the virion surface. These data provide a blueprint for the rational design of immunotherapeutics and vaccines capable of preventing RVFV infection and a model for understanding Ab-mediated neutralization of bunyaviruses more generally.
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