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An antigenic epitope is the specific chemical group or molecular surface feature on an antigen that is recognized by the variable regions (paratopes) of an antibody or B-cell receptor (Janeway et al., 2001). These epitopes are the primary targets for the adaptive immune system, enabling the identification of pathogens such as viruses and bacteria, as well as the recognition of aberrant self-cells in cancer (Sela-Culang et al., 2013). Epitopes are broadly classified into linear epitopes, which consist of a continuous sequence of residues, and conformational epitopes, which are formed by the three-dimensional folding of the antigen (Sela-Culang et al., 2013). In drug development, monoclonal antibodies are engineered to bind to specific epitopes with high affinity to achieve therapeutic effects, such as neutralizing viral entry or inhibiting the activity of pro-inflammatory cytokines (Lu et al., 2020). The selection of a target epitope is critical, as binding to epitopes shared with healthy tissues can lead to off-target toxicity and autoimmune reactions (Lu et al., 2020). Furthermore, the structural characterization of epitopes, known as epitope mapping, is essential for understanding the mechanism of action of therapeutic antibodies and for the design of effective vaccines (Sela-Culang et al., 2013).
Monoclonal antibodies bind to specific epitopes to neutralize pathogens, block receptor-ligand interactions, or induce immune effector functions such as antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) (Lu et al., 2020).
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