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The highly glycosylated glycoprotein spike of Ebola virus (EBOV-GP1,2) is the primary target of the humoral host response. Recombinant EBOV-GP ectodomain (EBOV-GP1,2ecto) expressed in mammalian cells was used to immunize sheep and elicited a robust immune response and produced high titers of high avidity polyclonal antibodies. Investigation of the neutralizing activity of the ovine antisera in vitro revealed that it neutralized EBOV. A pool of intact ovine immunoglobulin G, herein termed EBOTAb, was prepared from the antisera and used for an in vivo guinea pig study. When EBOTAb was delivered 6 hours after challenge, all animals survived without experiencing fever or other clinical manifestations. In a second series of guinea pig studies, the administration of EBOTAb dosing was delayed for 48 or 72 hours after challenge, resulting in 100% and 75% survival, respectively. These studies illustrate the usefulness of EBOTAb in protecting against EBOV-induced disease.

Original publication




Journal article


J Infect Dis

Publication Date





1124 - 1133


Ebola, antibody, efficacy, neutralization, therapeutic, Animals, Antibodies, Viral, Cost-Benefit Analysis, Ebolavirus, Female, Gene Expression Regulation, Viral, Glycoproteins, Guinea Pigs, HEK293 Cells, Hemorrhagic Fever, Ebola, Humans, Immunoglobulin G, Membrane Glycoproteins, Protein Binding, Protein Structure, Tertiary, Sheep, Viral Load