Recombinant polyclonal antibodies (rpAb) are a mixture of antibodies that bind to different regions of the same antigen or multiple antigens. The advantages of creating pAbs recombinantly over current antibody therapeutics are believed to be significant. The first generation of antibodies, immunoglobulins, display the diversity of the immune system. The second generation of antibodies, monoclonal antibodies, is highly specific. The third generation of antibodies, recombinant rpAb, mimics the natural immune system by combining specificity, diversity and naturally high affinity.

An important weapon in the human immune system’s fight against pathogens such as viruses and bacteria is the generation of a specific antibody response. Antibodies are Y-shaped proteins used by the immune system to identify and neutralize antigens, foreign entities that enter the human body. An antibody comprises both variable and constant regions. The variable region is responsible for recognizing a particular antigen. The constant region is responsible for inducing effector functions necessary to eliminate that antigen.

The immune system produces several different antibodies that bind to different structures on the surface of a given antigen. The diverse array of antibodies, or the “polyclonality” of the immune response, increases the likelihood that the antigens will be eliminated and is a key element in the immune systems effectiveness. The use of antibodies for prevention or treatment of diseases has become very attractive in recent years thanks to their high specificity, effectiveness and low adverse effects. Thus, clinicians and patients are capitalizing on nature’s own way to fight diseases.

Immunoglobulins, the first generation of antibody therapeutics, have been in medical use for more than a hundred years. Immunoglobulins are in general isolated from blood of healthy or vaccinated donors, and in certain cases animals or donors who have recovered from a specific disease. Unfortunately, immunoglobulins are associated with several disadvantages, including: low efficacy because only a fraction of the antibodies will be specific to a particular antigen, safety issues due to the risk of disease transmission, and supply shortage due to dependency on donor blood availability.

Monoclonal antibodies, the second generation of antibody therapeutics, have been in medical use since the late 1980s. While monoclonal antibodies overcome the above-mentioned shortfalls of immunoglobulins, they are only effective against diseases where a simple antigen is the cause. Because monoclonal antibodies bind to only one single structure out of many on the surface of a complex antigen, they are less likely to be able to completely neutralize or eliminate that antigen. Therefore, these therapeutics have limited effects in treatment of diseases caused by complex antigens, such as many cancers and infectious diseases.

Recombinant polyclonal antibodies, the third generation of antibody therapeutics, address the shortfalls of the first two generations by mimicking the diversity, specificity and binding capability of the natural human immune system. Symphogen’s proprietary polyclonal antibodies not only reflect the diversity of immunoglobulins, but also capture the specificity of monoclonal antibodies. Symphogen’s polyclonal antibodies are recombinant, making it possible to be produced in unlimited supply using traditional large-scale biological manufacturing techniques, with no risk of viral or prion transmission.