
An antibody is a protein produced by the immune system to recognize and neutralize specific antigens like viruses.Antibodies are glycoproteins of the immunoglobulin superfamily, produced by plasma cells (activated B-lymphocytes). Each antibody consists of two heavy and two light chains linked by disulfide bonds, and has a variable region for antigen recognition and a constant region that determines effector functions. There are five classes: IgM, IgG, IgA, IgE, IgD. Binding to an antigen can directly block infectivity, as well as opsonize the pathogen, activate complement and natural killer cells (antibody-dependent cellular cytotoxicity). Monoclonal antibodies are a key tool in biotechnology and medicine.
Antibody-based immunity was discovered by Emil von Behring and Shibasaburo Kitasato in 1890 with the demonstration of passive immunization against diphtheria toxin using serum. In 1959, Gerald Edelman and Rodney Porter independently determined the structure of antibodies, for which they received the Nobel Prize. The invention of monoclonal antibody technology by César Milstein and Georges Köhler in 1975 opened the era of therapeutic antibodies.
Antigen recognition is based on non-covalent interactions (hydrogen bonds, electrostatic, hydrophobic) between the hypervariable regions (CDRs) of the antibody and the antigenic epitope. Binding alters the antibody's conformation, and through the Fc fragment effector mechanisms are initiated: complement-dependent cytolysis (C1q is recruited to the Fc, triggering the cascade), antibody-dependent cellular cytotoxicity (FcγRIII on NK cells), opsonization of phagocytes. Different isotypes perform specialized functions: IgG is the main one in blood, IgA in mucous membranes, IgE in allergies and parasites. The principle of genetic recombination and selection underlies adaptive recognition.
Antibodies are used in therapy (e.g., against COVID-19), in diagnostic tests (pregnancy tests), and in scientific experiments to detect proteins.
The human body can produce more than a billion different antibodies, although the number of genes is relatively small — diversity is achieved through the shuffling of genetic segments.



