Structural Basis of Broad Ebolavirus Neutralization by a Human Survivor Antibody

@inproceedings{West2018StructuralBO,
  title={Structural Basis of Broad Ebolavirus Neutralization by a Human Survivor Antibody},
  author={Brandyn R West and Anna Z. Wec and Crystal L Moyer and Marnie L. Fusco and Philipp A Illinykh and Keta Huang and Rebekah M James and Andrew S Herbert and Sean Hui and Ariel S. Wirchnianski and Eileen Goodwin and Javad Jomepour Chehar Aman and Laura M Walker and John M Dye and Alexander Bukreyev and Kartik Chandran and Erica Ollmann Saphire},
  year={2018}
}
The structural features that govern broad-spectrum activity of broadly neutralizing, anti-ebolavirus antibodies (Abs) are currently unknown. Here we describe the first structure of a broadly neutralizing human Ab, ADI-15946, in complex with cleaved Ebola virus glycoprotein (EBOV GPCL). We find that ADI-15946 employs structural mimicry of a conserved interaction between the GP core and the glycan cap B17-B18 loop to inhibit infection. Both endosomal proteolysis of EBOV GP and binding of… CONTINUE READING