Antitestek

Antibodies, or immunoglobulins, are large glycoproteins produced mainly by plasma cells as part of the adaptive immune system. They recognize and bind to specific antigens, such as components of pathogens, toxins, or infected cells, helping to neutralize them and coordinate other immune responses. In Hungarian, the term antitestek is used to refer to these molecules.

Structurally, antibodies are Y-shaped molecules composed of two identical heavy chains and two identical light chains. The antigen-binding fragments (Fab) at the tips of the arms confer specificity, while the crystallizable fragment (Fc) mediates effector functions by interacting with immune cells and complement proteins. Antibodies are categorized into isotypes, including IgA, IgD, IgE, IgG, and IgM, each with distinct roles and distributions.

Antibody diversity arises from V(D)J gene rearrangement during B cell development, somatic hypermutation, and class switching. This allows recognition of a vast array of antigens while enabling changes in effector function without altering specificity.

The main mechanisms of action include neutralization of pathogens or toxins, opsonization to promote phagocytosis, activation of the complement system, and antibody-dependent cellular cytotoxicity. Antibodies also form the basis of many diagnostic tests and therapeutic approaches.

In diagnostics, antibodies are used in immunoassays, immunofluorescence, and Western blot assays to detect antigens or specific antibodies in patient samples. Therapeutically, monoclonal and polyclonal antibodies are employed to treat cancers, autoimmune diseases, infectious diseases, and to provide passive immunity.

Production methods include conventional hybridoma technology, recombinant engineering to create chimeric or humanized antibodies, and display technologies. Safety considerations include potential allergic reactions and, in rare cases, serum sickness with some animal-derived preparations.