Monoclonal Antibodies as Reagents

Abstract

Immunization of an animal by the standard procedure produces a polyclonal antibody response to many antigenic structures on an antigen as well as to any other contaminating materials in the antigen preparation. Therefore, one of the preconditions for obtaining specific antisera has been to highly purify the antigen. Very often, however, this requirement is impossible to satisfy especially with biological antigens. This is the case with viral preparations where knowledge and separation of complex biological molecules without destruction of native structure usually cannot be accomplished. About ten years ago, Kohler and Milstein described a technique that could overcome these problems and produce specific antibodies against previously unknown antigens never before available in a purified or enriched state. The technique involved the fusion of mouse myeloma cells with normal mouse spleen cells to produce hybrid cells called hybridomas [1]. These cells have the growth characteristics of the mouse tumor cells along with the capability of antibody production found in normal spleen cells. A single clone of these hybrid cells will produce and secrete a homogeneous monoclonal protein, i.e., monoclonal antibody. If the donor animal of the spleen cells has been previously inoculated with an antigen, the hybridoma cells produced after fusion will synthesize and secrete large volumes of various monoclonal antibodies with high specificity to the antigen.