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
The therapeutic efficacy of antibodies is closely related to their ability to recognize and bind specific epitopes on target antigens. Epitopes, or antigenic determinants, are a group of amino acids or other chemical groups that are part of a molecule to which an antibody attaches itself. Epitope characterization can help reveal the mechanism of antibody binding and apply intellectual property (patent) protection for novel antibodies, in addition to designing antibodies with high specificity and minimal cross-reactivity.
Understanding the differences between antibody specificity and selectivity is essential for designing and interpreting antibody-based assays in research for experimental accuracy and data interpretation. Antibody specificity refers to an antibody's ability to recognize and bind to a particular epitope—a unique part of an antigen that elicits an immune response.
Antibody-based assays are essential tools in biomedical research, providing the means to detect, quantify, and visualize specific proteins or antigens within complex biological samples. These assays' efficacy hinges on the antibodies' precise properties. While affinity, avidity, specificity, and selectivity are fundamental to antibody performance, the ultimate impact of these properties is heavily influenced by the experimental context in which the antibody is employed.
Biologics, particularly antibodies, have become indispensable in biomedical research and therapeutic development. Research-use-only (RUO) biologics play a pivotal role in preclinical studies, providing researchers with the necessary tools to explore antibody functions and therapeutic potential in vivo.
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