ResourcesBlogPros and Cons of Using Monoclonal Antibodies
Pros and Cons of Using Monoclonal Antibodies
Biointron2024-01-20Read time: 3 mins
Image credit: The Wellcome Trust
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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Antibodies are versatile molecules that perform a range of effector functions, many of which engage different arms of the immune system. Their modes of action extend beyond simple antigen binding, enabling the activation of various immune mechanisms that lead to pathogen neutralization and clearance. These functions include blocking molecular interactions, activating the complement system, and linking the humoral immune response to cellular immune responses via Fc receptor engagement.
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In addition to isotypes and subtypes, antibodies exhibit genetic variation known as allotypes, which are polymorphic epitopes on immunoglobulins. These allotypic differences arise from allelic variations in immunoglobulin genes, causing certain antibody subtypes to differ between individuals or ethnic groups. The presence of these polymorphic forms can influence immune responses, particularly when an individual is exposed to a non-self allotype, potentially triggering an anti-allotype immune reaction.
In mammals, antibodies are classified into five major isotypes: IgA, IgD, IgE, IgG, and IgM. Each isotype is defined by the heavy chain it contains: alpha (IgA), delta (IgD), epsilon (IgE), gamma (IgG), or mu (IgM). These structural differences in the heavy chains determine the antibody's function, tissue localization, and role in the immune response. Furthermore, antibody light chains fall into two classes—kappa and lambda—with kappa being more common, though both exhibit similar functions despite differences in sequence.
