Abstract
Abstract Ebola virus (EBOV) causes lethal hemorrhagic fevers with case fatality rates of up to 90%. The recent large outbreak in West Africa and current outbreak in the DRC demonstrate an obvious need for vaccines and therapeutics. All vaccine candidates use the surface glycoprotein as the main antigen. However, the method of protection induced by the EBOV glycoprotein remains unclear. The EBOV glycoprotein is composed of GP1 and GP2 linked by a disulfide bond. GP1 contains the receptor binding domain, glycan cap, and the heavily glycosylated mucin-like domain while GP2 contains the fusion loop and transmembrane anchor. We have developed a subunit vaccine that allows for an increased safety profile as well as shows increased thermostability, which allows easier deployment in central Africa. With our studies we expect to reveal antibody patterns differentiating survivors and non-survivors from non-human primate studies as well as reveal subdomains that are more protective and/or immunodominant to guide future vaccine development as well as provide insights into correlates of protection. Subunits of the EBOV glycoprotein have been produced in Drosophila S2 cells including full length GP, GPΔmucin-like domain, GP1, GP2, and sGP. These subdomains will be used to explore the binding patterns of antibodies elicited by a highly purified GP subunit vaccine. Ongoing analysis focuses on samples from non-human primates immunized with 3 doses of EBOV GP + adjuvant that will be analyzed for antigen binding IgG to differentiate the pre-challenge antibody binding patterns to the different EBOV subdomains.
Published Version
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