Structural and molecular basis for Ebola virus neutralization by protective human antibodies
- 18 March 2016
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 351 (6279) , 1343-1346
- https://doi.org/10.1126/science.aad6117
Abstract
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 & 1343Keywords
Funding Information
- Intramural Research Program of the Vaccine Research Center
- National Institute of Allergy and Infectious Diseases
- NIH (NIH-5K08AI079381)
- Boston Children's Hospital Faculty Development
- National Institute of General Medical Sciences of the National Institutes of Health (T32GM008704)
- 973 Program (2015CB14010102)
- National Natural Science Foundation of China (81550001, 31470721)
- Junior Thousand Talents Program of China (20131770418)
- Frederick National Laboratory for Cancer Research
- National Institutes of Health (HHSN261200800001E)
This publication has 54 references indexed in Scilit:
- Mechanism of Human Antibody-Mediated Neutralization of Marburg VirusCell, 2015
- Reversion of advanced Ebola virus disease in nonhuman primates with ZMappNature, 2014
- Conserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza VirusesJournal of Virology, 2014
- Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domainsProceedings of the National Academy of Sciences, 2014
- How good are my data and what is the resolution?Acta Crystallographica Section D-Biological Crystallography, 2013
- Cathepsin Cleavage Potentiates the Ebola Virus Glycoprotein To Undergo a Subsequent Fusion-Relevant Conformational ChangeJournal of Virology, 2012
- iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLMActa Crystallographica Section D-Biological Crystallography, 2011
- Phasercrystallographic softwareJournal of Applied Crystallography, 2007
- Endosomal Proteolysis of the Ebola Virus Glycoprotein Is Necessary for InfectionScience, 2005
- Accurate determination of local defocus and specimen tilt in electron microscopyJournal of Structural Biology, 2003