Role of Helical Structure in MBP Immunodominant Peptides for Efficient IgM Antibody Recognition in Multiple Sclerosis
- PMID: 35795217
- PMCID: PMC9250970
- DOI: 10.3389/fchem.2022.885180
Role of Helical Structure in MBP Immunodominant Peptides for Efficient IgM Antibody Recognition in Multiple Sclerosis
Abstract
The involvement of Myelin Basic Protein (MBP) in Multiple Sclerosis (MS) has been widely discussed in the literature. This intrinsically disordered protein has an interesting α-helix motif, which can be considered as a conformational epitope. In this work we investigate the importance of the helical structure in antibody recognition by MBP peptides of different lengths. Firstly, we synthesized the peptide MBP (81-106) (1) and observed that its elongation at both N- and C-termini, to obtain the peptide MBP (76-116) (2) improves IgM antibody recognition in SP-ELISA, but destabilizes the helical structure. Conversely, in competitive ELISA, MBP (81-106) (1) is recognized more efficiently by IgM antibodies than MBP (76-116) (2), possibly thanks to its more stable helical structure observed in CD and NMR conformational experiments. These results are discussed in terms of different performances of peptide antigens in the two ELISA formats tested.
Keywords: NMR; circular dichroism; immune response; multiple sclerosis; myelin basic protein antigen; peptide-antigen based ELISA; synthetic helical peptides.
Copyright © 2022 Staśkiewicz, Quagliata, Real-Fernandez, Nuti, Lanzillo, Brescia-Morra, Rusche, Jewginski, Carotenuto, Brancaccio, Aharoni, Arnon, Rovero, Latajka and Papini.
Conflict of interest statement
Author HR is employed by Fischer Analytics GmbH. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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