Monoclonal antibodies (mAbs) are immunoglobulins obtained from single cloned homogeneous hybrid cells (B lymphocyte cells). This is done by fusing spleen cells of an antigen-exposed mouse with human or mouse myeloma cells, then cloning the hybridomas to produce the desired single antibody clone.
They are used for diagnosis and treatment in various therapeutic areas, including cancer, infectious viral, and bacterial diseases. mAbs can bind to pathogens to reduce their capability to infect new cells, or bind to receptors of microbes, abnormal cells, and proteins, thus preventing escalation of the disease-state and subsequent infections.1 However, mAbs have several pros and cons when being considered for research.
Pros
Binds with high specificity due to being products of a single clone, and most mAbs do not show cross-reactivity.
Multiple uses (incl. diagnostic assays, therapies) and treats a wide range of conditions.
Hybridoma cells which produce mAbs are perpetual sources of antibodies with the same specificity and sensitivity.
Can be used with or without purification.
Very useful for conjugation to different probes as their homogenous chemical nature can be characterized easily.
Side effects of mAb drugs can be treated through optimization, such as humanization or affinity maturation, or by using antibody fractions.
Cons
More expensive than polyclonal antibodies.
Production requires both in vivo and in vitro systems due to laborious process of producing immortalized hybridoma cell lines.
Skilled and trained workers are essential.
Potential adverse effects when used in therapeutics if human anti-monoclonal antibody (HAMA) response is triggered.
Due to its homogeneity, mAbs are vulnerable to degradation because of the shared susceptibility among all antibody molecules within the solution.
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Singh, A., Chaudhary, S., Agarwal, A., & Verma, A. S. (2014). Antibodies: Monoclonal and Polyclonal. Animal Biotechnology, 265-287. https://doi.org/10.1016/B978-0-12-416002-6.00015-8
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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