Malondialdehyde-lysine oxidation-specific epitope (MDA-Lys OSE)

Malondialdehyde-lysine (MDA-Lys) oxidation-specific epitopes (OSEs) are neoantigens formed when malondialdehyde, a reactive byproduct of lipid peroxidation, covalently modifies lysine residues on proteins such as Apolipoprotein B-100 (Witztum & Lichtman, 2014). These epitopes are recognized by the innate immune system as damage-associated molecular patterns (DAMPs) through scavenger receptors (e.g., CD36) and natural antibodies, such as IgM (Miller et al., 2011). In atherosclerotic tissue, the accumulation of MDA-Lys OSEs promotes the recruitment of inflammatory cells and the transformation of macrophages into foam cells, driving plaque progression and instability (Tsimikas & Hall, 2010). Therapeutic strategies targeting these epitopes, such as the monoclonal antibody Ordesekimab (BI 655088), aim to neutralize their pro-inflammatory signaling and facilitate the non-inflammatory clearance of oxidized lipids (Binder et al., 2016). Beyond cardiovascular disease, MDA-Lys epitopes serve as critical biomarkers for oxidative stress and are implicated in the pathogenesis of other inflammatory conditions, including nonalcoholic steatohepatitis and neurodegenerative diseases (Sun et al., 2018).

Other names

MDA-modified LDLMalondialdehyde-modified lysineMDA-adductsMDA-LysMalondialdehyde-lysine adduct

Neutralization of pro-inflammatory epitopes and inhibition of macrophage-mediated uptake of oxidized lipoproteins to prevent foam cell formation.