ArticleHuman vaccines & immunotherapeutics2017
Epitope mapping of Ebola virus dominant and subdominant glycoprotein epitopes facilitates construction of an epitope-based DNA vaccine able to focus the antibody response in mice.
Article in Human vaccines & immunotherapeutics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 16 citations in OpenAlex.
- Oriented Multivalent Display Drives Consistent Serum Immunodominance to the Ebola Virus Glycoprotein.ACS central science · 2026Article
- Single dose VSV-based vaccine protects mice against lethal heterologous Crimean-Congo hemorrhagic fever virus challenge.NPJ vaccines · 2025Article
- A comprehensive investigation of Glycoprotein-based nucleic acid vaccines for Hantaan Virus.NPJ vaccines · 2024Article
- Article
- A conserved epitope in VAR2CSA is targeted by a cross-reactive antibody originating fromFrontiers in cellular and infection microbiology · 2023Article
- A live-attenuated viral vector vaccine protects mice against lethal challenge with Kyasanur Forest disease virus.NPJ vaccines · 2021Article
- Ebola vaccine-induced protection in nonhuman primates correlates with antibody specificity and Fc-mediated effects.Science translational medicine · 2021Article
- Generation of a Peptide Vaccine Candidate against Falciparum Placental Malaria Based on a Discontinuous Epitope.Vaccines · 2020Article
- The Case for Exploiting Cross-Species Epitopes in Malaria Vaccine Design.Frontiers in immunology · 2020Review
- Article
- Combinatorial peptide-based epitope mapping from Ebola virus DNA vaccines and infections reveals residue-level determinants of antibody binding.Human vaccines & immunotherapeutics · 2017Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We performed epitope mapping studies on the major surface glycoprotein (GP) of Ebola virus (EBOV) using Chemically Linked Peptides on Scaffolds (CLIPS), which form linear and potential conformational epitopes. This method identified monoclonal antibody epitopes and predicted additional epitopes recognized by antibodies in polyclonal sera from animals experimentally vaccinated against or infected with EBOV. Using the information obtained along with structural modeling to predict epitope accessibility, we then constructed 2 DNA vaccines encoding immunodominant and subdominant epitopes predicted to be accessible on EBOV GP. Although a construct designed to produce a membrane-bound oligopeptide was poorly immunogenic, a construct generating a secreted oligopeptide elicited strong antibody responses in mice. When this construct was administered as a boost to a DNA vaccine expressing the complete EBOV GP gene, the resultant antibody response was focused largely toward the less immunodominant epitopes in the oligopeptide. Taken together, the results of this work suggest a utility for this method for immune focusing of antibody responses elicited by vaccination.
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