6I9I
Rift valley fever virus Gn in complex with a neutralizing antibody fragment
Summary for 6I9I
| Entry DOI | 10.2210/pdb6i9i/pdb |
| Descriptor | RV-Gn1 Heavy chain, RV-Gn1 Light chain, Glycoprotein, ... (4 entities in total) |
| Functional Keywords | glycoprotein, antibody, phlebovirus, neutralization, viral protein |
| Biological source | Oryctolagus cuniculus More |
| Total number of polymer chains | 6 |
| Total formula weight | 165021.10 |
| Authors | Allen, E.R.,Bowden, T.A. (deposition date: 2018-11-23, release date: 2018-12-26, Last modification date: 2024-11-06) |
| Primary citation | Allen, E.R.,Krumm, S.A.,Raghwani, J.,Halldorsson, S.,Elliott, A.,Graham, V.A.,Koudriakova, E.,Harlos, K.,Wright, D.,Warimwe, G.M.,Brennan, B.,Huiskonen, J.T.,Dowall, S.D.,Elliott, R.M.,Pybus, O.G.,Burton, D.R.,Hewson, R.,Doores, K.J.,Bowden, T.A. A Protective Monoclonal Antibody Targets a Site of Vulnerability on the Surface of Rift Valley Fever Virus. Cell Rep, 25:3750-3758.e4, 2018 Cited by PubMed 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. PubMed: 30590046DOI: 10.1016/j.celrep.2018.12.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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