Monoclonal Antibodies in Paediatric Acute Lymphoblastic Leukemia

Abstract

In 1975, Kohler et al. produced the first monoclonal antibodies (moAbs) by fusing a myeloma cell line with a specific antibody-producing B cell. This combined the unlimited growth potential of myeloma cells with the predetermined antibody specificity of normal immune spleen cells from an immunized mouse. The technique called somatic cell hybridization results in a hybridoma [1]. Humans receiving murine moAbs produce human anti-mouse antibodies (HAMA) leading to inactivation of the moAbs and allergic complications. The chimerization or humanization of moAbs via innovative recombinant DNA technology leads to a better tolerance to the compounds and has allowed for using the natural effector mechanisms of destroying with moAb-coated targets [2]. Whereas chimeric moAbs have antigenbinding parts (variable regions) of the mouse antibody and the effector parts (constant region, Fc) of a human antibody, in humanized compounds the mousederiving part of the moAb is reduced to the antigen-binding site (hypervariable region). The methodological approach to engineer the composition of moAbs is a broad and intensively developing field [3]. Structure of Monoclonal Antibodies (moAbs)A physiological IgG antibody consists of four polypeptide chains, two identical heavy chains and two identical light chains, which are covalently linked by interchain disulfide bonds. The chains have a variable (V) and a constant (C) region. The constant region of light chains consists of one C-domain, and the heavy chains have A. von Stackelberg (*) Pädiatrische Onkologie/Hämatologie,