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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	A protective monoclonal antibody targets a site of vulnerability on the surface of Rift Valley Fever Virus Elizabeth R. Allen , Stefanie A. Krumm , Jayna Raghwani , Steinar Halldorsson , Angela Elliott , Victoria A. Graham , Elina Koudriakova , Karl Harlos , Daniel Wright , George M. Warimwe , Benjamin Brennan , Juha T. Huiskonen , Stuart D. Dowall , Richard M. Elliott , Oliver G. Pybus , Dennis R. Burton , Roger Hewson , Katie J. Doores , Thomas A. Bowden Cell Reports 25, 3750 - 3758.e4 DOI: 10.1016/j.celrep.2018.12.001 Diamond Proposal Number(s): [14744] Open Access Show Abstract ▼ Abstract: 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 RVFV Gn 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.	Dec 2018

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I03-Macromolecular Crystallography

A protective monoclonal antibody targets a site of vulnerability on the surface of Rift Valley Fever Virus