ArticleMolecular immunology2010
Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes.
Article in Molecular immunology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Bacteriophages as a modern diagnostic tool: innovations, applications and challenges.Molecular biology reports · 2025Review
- Antibodies and cryptographic hash functions: quantifying the specificity paradox.Frontiers in immunology · 2025Article
- Computational identification of antibody-binding epitopes from mimotope datasets.Frontiers in bioinformatics · 2024Article
- Protein Nanoparticle-Mediated Delivery of Recombinant Influenza Hemagglutinin Enhances Immunogenicity and Breadth of the Antibody Response.ACS infectious diseases · 2023Article
- Benchmarking the PEPOP methods for mimicking discontinuous epitopes.BMC bioinformatics · 2019Article
- PEPOP 2.0: new approaches to mimic non-continuous epitopes.BMC bioinformatics · 2019Article
- Strategies for Generating Diverse Antibody Repertoires Using Transgenic Animals Expressing Human Antibodies.Frontiers in immunology · 2018Article
- Construction and immunogenicity of a recombinant swinepox virus expressing a multi-epitope peptide for porcine reproductive and respiratory syndrome virus.Scientific reports · 2017Article
- Affinity selection of epitope-based vaccines using a bacteriophage virus-like particle platform.Current opinion in virology · 2015Review
- Beyond phage display: non-traditional applications of the filamentous bacteriophage as a vaccine carrier, therapeutic biologic, and bioconjugation scaffold.Frontiers in microbiology · 2015Review
- Anti-idiotypic monobodies for immune response profiling.Methods (San Diego, Calif.) · 2012Article
- B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study.Nature biotechnology · 2012Article
- Antigen-antibody interface properties: composition, residue interactions, and features of 53 non-redundant structures.Biochimica et biophysica acta · 2012Article
- Complex binding sites made to order.Nature biotechnology · 2012Article
- Requirements for empirical immunogenicity trials, rather than structure-based design, for developing an effective HIV vaccine.Archives of virology · 2012Review
- Basic research in HIV vaccinology is hampered by reductionist thinking.Frontiers in immunology · 2012Article
- The epitope and neutralization mechanism of AVFluIgG01, a broad-reactive human monoclonal antibody against H5N1 influenza virus.PloS one · 2012Article
- A general insert label for peptide display on chimeric filamentous bacteriophages.Analytical biochemistry · 2012Article
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Authors and funding
7 authors.
Funding
Abstract
Peptide "mimics" (mimotopes) of linear protein epitopes and carbohydrate epitopes have been successfully used as immunogens to elicit cross-reactive antibodies against their cognate epitopes; however, immunogenic mimicry has been difficult to achieve for discontinuous protein epitopes. To explore this, we developed from phage-displayed peptide libraries optimized peptide mimics for three well-characterized discontinuous epitopes on hen egg lysozyme and horse cytochrome c. The peptides competed with their cognate antigens for antibody binding, displayed affinities in the nM range, and shared critical binding residues with their native epitopes. Yet, while immunogenic, none of the peptides elicited antibodies that cross-reacted with their cognate antigens. We analyzed the 3-D structure of the site within each discontinuous epitope that shared critical binding residues with its peptide mimic, and observed that in each case it formed a ridge-like patch on the epitope; in no case did it cover most or all of the epitope. Thus, the peptides' lack of immunogenic mimicry could be attributed to their inability to recapitulate the topological features of their cognate epitopes. Our results suggest that direct peptide immunizations are not a practical strategy for generating targeted antibody responses against discontinuous epitopes.
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