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A linear B-cell epitope is a contiguous sequence of amino acids within an antigen that is recognized and bound by the antigen-binding site of a B-cell receptor or antibody[1][5][8]. Unlike conformational epitopes, which are formed by amino acids brought together upon protein folding, linear epitopes consist of a continuous stretch of residues and are determined primarily by their primary sequence and to some extent by local structure[1][5]. These epitopes drive humoral immunity as their recognition triggers antibody production, and they are essential in vaccine design, immunodiagnostics, and research studies investigating immune responses[1][9][10]. While important in biomedical sciences, the term "linear B-cell epitope" does not refer to a singular therapeutic target or protein, but rather to a class of antigenic segments relevant for antibody recognition[1][5][8].
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