Structural and molecular basis for Ebola virus neutralization by protective human antibodies

• DOI: 10.1126/science.aad6117
• Publication Date: 2016-02-26T04:23:35Z
• Authors: John Misasi; Morgan S. A. Gilman; Masaru Kanekiyo; Miao Gui; Alberto Cagigi; Sabue Mulangu; Davide Corti; Julie E. Ledgerwood; Antonio Lanzavecchia; James Cunningham; Jean Jacques Muye...; Ulrich Baxa; Barney S. Graham; Ye Xiang; Nancy J. Sullivan; Jason S. McLellan
• Keywords: 0303 health sciences; Protein Conformation; Cryoelectron Microscopy; Antibodies, Monoclonal; Hemorrhagic Fever, Ebola; Antibodies, Viral; Crystallography, X-Ray; Ebolavirus; Antibodies, Neutralizing; Cathepsins; 3. Good health; 03 medical and health sciences; Viral Envelope Proteins; Proteolysis; Humans

Antibodies block Ebola virus entry

The recent Ebola virus outbreak in West Africa illustrates the need for both an effective vaccine and therapies to treat infected individuals. Corti et al. isolated two monoclonal antibodies from a survivor of the 1995 Kikwit outbreak and demonstrated their therapeutic efficacy in Ebola virus–infected macaques. In fact, one antibody protected macaques when it was given up to 5 days after infection. Misasi et al. solved the crystal structures of fragments of the two antibodies bound to the Ebola virus glycoprotein (GP), which mediates viral cell entry. The two antibodies targeted different regions of GP, but in both cases blocked steps required for viral entry.

Science , this issue pp. 1339 & 1343