EMD-6527

Single-particle
17.0 Å
EMD-6527 Deposition: 20/11/2015
Map released: 06/04/2016
Last modified: 06/04/2016
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-6527

Negative stain EM reconstruction of Bundibugyo virus (BDBV) glycoprotein in complex with a human IgG1 Fab

EMD-6527

Single-particle
17.0 Å
EMD-6527 Deposition: 20/11/2015
Map released: 06/04/2016
Last modified: 06/04/2016
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens, Ebola virus sp.
Sample: Fab fragment of BDBV335 human IgG1 monoclonal antibody to Bundibugyo virus in complex with mucin-deleted Bundibugyo virus GP

Deposition Authors: Flyak AI , Shen X, Murin CD, Turner HL, Fusco ML, Lampley R, Kose N, Ilinykh PA, Kuzmina N , Branchizio A, King H, Brown L, Davidson E, Doranz BJ, Slaughter JC , Sapparapu G , Klages C, Ksiazek TG, Saphire EO , Ward AB, Bukreyev A, Crowe JE
Cross-Reactive and Potent Neutralizing Antibody Responses in Human Survivors of Natural Ebolavirus Infection.
Abstract:
Recent studies have suggested that antibody-mediated protection against the Ebolaviruses may be achievable, but little is known about whether or not antibodies can confer cross-reactive protection against viruses belonging to diverse Ebolavirus species, such as Ebola virus (EBOV), Sudan virus (SUDV), and Bundibugyo virus (BDBV). We isolated a large panel of human monoclonal antibodies (mAbs) against BDBV glycoprotein (GP) using peripheral blood B cells from survivors of the 2007 BDBV outbreak in Uganda. We determined that a large proportion of mAbs with potent neutralizing activity against BDBV bind to the glycan cap and recognize diverse epitopes within this major antigenic site. We identified several glycan cap-specific mAbs that neutralized multiple ebolaviruses, including SUDV, and a cross-reactive mAb that completely protected guinea pigs from the lethal challenge with heterologous EBOV. Our results provide a roadmap to develop a single antibody-based treatment effective against multiple Ebolavirus infections.