The field of antibody production has witnessed significant technological advancements over the past years, particularly in hybridoma technology, which remains a cornerstone for monoclonal antibody (mAb) production.
Electrofusion Technology in Hybridoma Preparation
Electrofusion technology can be applied as a cell engineering technique for hybridoma preparation. This method offers substantial improvements in efficiency and control over traditional polyethylene glycol-mediated cell fusion. Electrofusion involves electric field intensity, number of pulses, and pulse duration. However, key challenges in adopting electrofusion include selecting appropriate instruments, optimizing electrical parameters, and precisely controlling cell conditions. Despite this, electrofusion represents a promising advancement for enhancing the specificity and yield of monoclonal antibodies.1
Hybridoma Cell Screening and Expansion
The process of generating monoclonal antibodies through hybridoma technology involves screening hybridoma cells to select those producing the desired antibodies. This is typically achieved using enzyme-linked immunosorbent assay (ELISA) techniques, among others, to identify antibodies with the right specificity. Following screening, hybridomas that produce the desired antibodies are cloned and propagated to obtain stable cell populations for large-scale antibody production. This expansion can be performed either in vitro, using tissue culture techniques, or in vivo, by inoculating hybridoma cells into the abdomen of a mouse. However, the technology is not without limitations, such as long production times, resource-intensive processes, susceptibility to contamination, and challenges in generating short peptides and fragment antigens.
Clinical Significance and Applications
Hybridoma technology's clinical significance is vast, providing monoclonal antibodies for various diagnostic tests, cancer treatments, and research applications. The specificity and reliability of monoclonal antibodies produced via hybridoma technology have made it an indispensable tool in the diagnosis and treatment of numerous diseases. This technology enables the production of antibodies for detecting foreign antigens, identifying different strains of pathogens, and even treating viral diseases such as AIDS. Moreover, monoclonal antibodies are instrumental in radioimmunodetection and radioimmunotherapy of cancer, highlighting their critical role in modern medicine.2 Biointron offers hybridoma sequencing services for antibody discovery and production.
References:
Kou, J., Shen, J., Wang, Z., & Yu, W. (2023). Advances in hybridoma preparation using electrofusion technology. Biotechnology Journal, 18(10), 2200428. https://doi.org/10.1002/biot.202200428
Mitra, S., & Tomar, P. C. (2021). Hybridoma technology; advancements, clinical significance, and future aspects. Journal of Genetic Engineering and Biotechnology, 19(1), 1-12. https://doi.org/10.1186/s43141-021-00264-6
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.
