Monoclonal antibodies are synthetic proteins developed for therapeutic use in patients with a range of serious conditions, including Ebola, cancer, and COVID-19. Monoclonal antibodies are produced in a laboratory setting like any other therapeutic approach or medication. However, they work to fight illness by targeting and neutralizing disease-causing antigens, just like the natural antibodies inside the human immune system.
Monoclonal Antibodies vs. Natural Antibodies
The power of monoclonal antibodies lies in the way they target a specific and essential component of the process of infection. Like the natural antibodies produced in the human immune system, correctly prescribed monoclonal antibodies can target specific antigens and efficiently neutralize them. Monoclonal antibodies can be developed by exposing white blood cells to a target virus. The resulting antibodies can then be produced on a mass scale through a cloning process. Monoclonal antibody treatment is typically administered intravenously and can be done in a clinical setting or as an outpatient procedure.
Monoclonal antibodies can be thought of as a manufactured alternative to (or supplement for) naturally occurring antibodies and are designed to mimic their natural counterparts closely. In common therapeutic applications, monoclonal antibodies are given to a patient to boost or otherwise affect their natural immune system. They may also act as a replacement for natural antibodies in persons who are unable to produce them because of an autoimmune condition.
Monoclonal Antibodies for the Treatment of COVID-19
In 2020, the United States Food and Drug Administration (FDA) issued emergency authorization for monoclonal antibodies to be used as a treatment for COVID-19. Monoclonal antibody treatment has shown promise in reducing the risk of severe infection and hospitalization in high-risk COVID-19 patients, especially when antibody treatment begins immediately after diagnosis.
The spiky shape of the COVID-19 virus has become ubiquitous in the public consciousness through health department posters, news segments, and memes and can be attributed to the presence of spike proteins on the surface of the virus. These spike proteins make COVID-19 highly effective at attaching to human cells. It is also the feature that makes COVID-19 a suitable candidate for treatment with monoclonal antibodies.
Multiple monoclonal antibodies have been developed with the specific goal of binding to coronavirus spike proteins. They have been demonstrated to be effective in disabling the virus and undermining its ability to bind to and enter human cells. Monoclonal antibody treatment has remained effective against COVID-19 variants thus far. However, there is potential that future mutations of the COVID-19 virus could see significant changes in the shape of the spike protein structure. This could make existing monoclonal antibodies less effective, and continued research is necessary to maintain the efficacy of antibody treatment.