monoclonal antibody

monoclonal antibody, an antibody that is mass produced in the laboratory from a single clone and that recognizes only one antigen. Monoclonal antibodies are typically made by fusing a normally short-lived, antibody-producing B cell (see immunity) to a fast-growing cell, such as a cancer cell (sometimes referred to as an “immortal” cell). The resulting hybrid cell, or hybridoma, multiplies rapidly, creating a clone that produces large quantities of the antibody.

Monoclonal antibodies engendered much excitement in the medical world and in the financial world in the 1980s, especially as potential cures for cancer. They have been used in laboratory research and in medical tests since the mid-1970s, but their effectiveness in disease treatment was limited especially by the tendency of the early monoclonal antibodies to provoke an immune response against them because of the use of mouse cells in creating the hybridoma. This problem has been overcome through the use of recombinant DNA to produce chimeric and humanized monoclonal antibodies and of transgenic mice and other techniques to produce human antibodies. Monoclonal antibody therapies have been developed to treat transplant rejection, some autoimmune diseases, some types of lymphoma, leukemia, and breast and other cancers, and Ebola virus disease. These therapies use monoclonal antibodies in variety of ways. The antibodies may home in on specific antigens found on the surface of targeted cells to deliver radioactive materials, drugs or inactive drug precursors (subsequent converted to a drug by an enzyme), tumor-suppressing genes, or substances that suppress or inhibit signaling molecules involved in disease processes. Other antibodies bind to sites that enable viruses to infect cells, thus interfering with the infection process.

See study by L. V. Marks (2015).

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