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Epitopes of naturally acquired and vaccine-induced anti-Ebola virus glycoprotein antibodies in single amino acid resolution

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Heidepriem,  Jasmin
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Löffler,  Felix F.
Felix Löffler, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Heidepriem, J., Krähling, V., Dahlke, C., Wolf, T., Klein, F., Addo, M. M., et al. (2020). Epitopes of naturally acquired and vaccine-induced anti-Ebola virus glycoprotein antibodies in single amino acid resolution. Biotechnology Journal, 2000069. doi:10.1002/biot.202000069.


Cite as: https://hdl.handle.net/21.11116/0000-0006-823F-1
Abstract
Abstract The Ebola virus (EBOV) can cause severe infections in humans, leading to a fatal outcome in a high percentage of cases. Neutralizing antibodies against the EBOV surface glycoprotein (GP) can prevent infections, demonstrating a straightforward way for an efficient vaccination strategy. Meanwhile, many different anti-EBOV antibodies have been identified, whereas the exact binding epitopes are often unknown. Here, we present the analysis of serum samples from an EBOV vaccine trial with the viral vector vaccine rVSV-ZEBOV and an Ebola virus disease (EVD) survivor, using high-density peptide arrays. In this proof-of-principle study, we detected distinct IgG and IgM antibodies binding to different epitopes of EBOV GP: By mapping the whole GP as overlapping peptide fragments, we found new epitopes and confirmed epitopes from the literature. Furthermore, we could validate the highly selective binding epitope of a neutralizing monoclonal anti-EBOV GP antibody. This shows that peptide arrays can be a valuable tool to study the humoral immune response to vaccines in patients and to support Ebola vaccine development. This article is protected by copyright. All rights reserved