mAbs

Monoclonal antibodies (mAbs) are antibodies produced by identical immune cells cloned from a single parent cell and designed to bind with high specificity to a single antigenic epitope. They are generated using hybridoma techniques or recombinant methods. The concept emerged in 1975 from the work of Georges Köhler and César Milstein, who fused antibody-producing B cells with myeloma cells to create immortalized clones; this achievement earned the 1984 Nobel Prize in Physiology or Medicine.

mAbs can act through several mechanisms. They can neutralize or block receptor signaling, recruit immune effector functions such as antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC), deliver cytotoxic payloads as antibody-drug conjugates (ADCs), or engage T cells through bispecific formats (BiTEs). Their high specificity allows targeted intervention with relatively favorable safety profiles compared with broad-spectrum therapies.

Production and development have evolved from murine antibodies to chimeric, humanized, and fully human antibodies. Modern methods include recombinant DNA, phage display, and the use of transgenic animals. Manufacturing is typically in mammalian cell culture to ensure proper folding and glycosylation, followed by purification under Good Manufacturing Practice and rigorous quality control, with regulatory oversight across clinical trial phases.

Applications span therapeutics in oncology, autoimmune and inflammatory diseases, and infectious diseases, as well as diagnostic and research reagents. Examples include anti-CD20 antibodies for B-cell lymphomas, anti-HER2 antibodies for breast cancer, anti-PD-1 antibodies for various cancers, and anti-TNF therapies for autoimmune conditions.

Safety and challenges include infusion reactions, potential immunogenicity, and resistance development. Costs, complex manufacturing, and the need for biosimilars influence accessibility and ongoing regulatory evaluation.