Antigenic properties of peptidic mimics for epitopes of the lipopolysaccharide from Brucella
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Updated: Oct 18, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
X De Bolle1, T Laurent, A Tibor
1Immunology and Microbiology Laboratory, Research Unit in Molecular Biology (URBM), University of Namur (FUNDP), 61 rue de Bruxelles, Namur, B5000, Belgium. xavier.debolle@fundp.ac.be
Abstract:
The lipopolysaccharide (LPS) is up to now the only identified major virulence determinant of Brucella. This bacterium is responsible for brucellosis in animals and for Malta fever in humans. Several monoclonal antibodies (mAbs) directed against various LPS epitopes have been characterized. Two mAbs, named A15-6B3 and B66-2C8, directed against distinct LPS epitopes have been used to select peptides from 11 phage display libraries. The sequences of the selected peptides contain an overrepresentation of either proline or tryptophan residues when selected with either A15-6B3 or B66-2C8 mAbs, respectively. For the best binding peptides, competition with LPS for the binding to the mAb is detected, which suggests that the peptides bind to the paratope of the mAb. The phages selected from the libraries were used to immunise mice, and a weak antibody response directed against LPS has been observed. These data suggest that a subset of the selected peptides are mimotopes of the LPS epitopes.
Insights
Researchers identified peptides that mimic Brucella lipopolysaccharide (LPS) epitopes using phage display. These mimotopes could aid in developing diagnostics or vaccines for brucellosis and Malta fever.
Area of Science:
- Immunology
- Microbiology
- Bacteriology
Background:
- Lipopolysaccharide (LPS) is the primary virulence factor identified in Brucella, a bacterium causing brucellosis in animals and Malta fever in humans.
- Monoclonal antibodies (mAbs) targeting distinct LPS epitopes have been developed and characterized.
Purpose of the Study:
- To identify peptide mimotopes of Brucella LPS epitopes using phage display technology.
- To investigate the binding characteristics of selected peptides to anti-LPS monoclonal antibodies.
Main Methods:
- Phage display libraries were screened using two specific anti-LPS monoclonal antibodies (mAbs), A15-6B3 and B66-2C8.
- Selected peptides were analyzed for amino acid composition, and their binding was assessed through competition assays with LPS.
- Mice were immunized with selected phages to evaluate the immunogenicity of the peptide mimotopes.
Main Results:
- Peptide selection revealed an overrepresentation of proline residues with A15-6B3 mAb and tryptophan residues with B66-2C8 mAb.
- Competition assays demonstrated that the selected peptides bind to the antibody's paratope, indicating mimicry of LPS epitopes.
- Immunization of mice with selected phages elicited a weak antibody response against Brucella LPS.
Conclusions:
- A subset of peptides selected via phage display function as mimotopes of Brucella LPS epitopes.
- These mimotopes hold potential for further research in diagnostics and vaccine development for Brucella infections.
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