Phage display technology is a powerful technique for antibody discovery. It is often used to identify high-affinity interactions between antibody fragments (e.g. VHHs) and target proteins for the production of monoclonal antibodies. Originally developed in the mid-1980s, phage display is a key technology for antibody engineering, drug discovery, protein-protein interactions, and vaccine development.1
By genetically engineering the bacteriophage's coat protein, the VHH (heavy-domain camelid antibody fragment) sequence can be linked to the phage DNA, enabling the displayed antibody fragment to be encoded by the viral genome. This facilitates the production of a diverse library of phage particles, each carrying a different antibody fragment on its surface.
These phage display libraries screen the phage particles to identify antibodies that bind to specific target antigens in a process called panning, which involves repeated rounds of binding, washing, elution, and amplification. Once identified, these antibodies can be further optimized for improved affinity, specificity, and therapeutic properties. Additionally, phage display has facilitated the discovery of small peptide-based drugs and the identification of potential drug targets.
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References:
Hammers, C. M., & Stanley, J. R. (2014). Antibody Phage Display: Technique and Applications. The Journal of Investigative Dermatology, 134(2), e17. https://doi.org/10.1038/jid.2013.521
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.
