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The Inducible System: History of Development of Immunology as a Component of Host-Parasite Interactions
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
Antibodies are protein molecules secreted by B lymphocytes after they have encountered antigen. Each lymphocyte and its clonal descendants are capable of secreting only one type of specific antibody. The invading antigen “selects” the matching clone which then proliferates and differentiates into antibody-secreting plasma cells. Elucidation of the structure of the antibody molecule by analytical chemistry and use of the techniques of molecular biology to study the genome led to the discovery that genes undergo extensive recombination of their DNA in order to generate the remarkable antibody diversity that B lymphocytes possess. Since antigens are complex, many different clones are activated and many different antibodies are produced in an immune response to any antigenic exposure. The artificial production of hybridomas, however, allows for the production of monoclonal antibodies.
Antibody-Based Therapies
Published in David E. Thurston, Ilona Pysz, Chemistry and Pharmacology of Anticancer Drugs, 2021
Hybridoma technology involves the formation of hybrid cell lines (called “hybridomas”) by fusing a specific antibody-producing B cell with a myeloma (i.e., B-cell cancer) cell that is selected for its ability to grow in tissue culture and for an absence of antibody chain synthesis (Figure 7.4). The antibodies produced by the hybridoma are all of a single specificity and are therefore monoclonal in contrast to polyclonal antibodies.
Breast Imaging with Radiolabeled Antibodies
Published in Raymond Taillefer, Iraj Khalkhali, Alan D. Waxman, Hans J. Biersack, Radionuclide Imaging of the Breast, 2021
Lamk M. Lamki, Bruce J. Barron
Polyclonal antibodies have been used much earlier than monoclonal, but unfortunately, they have a problem of diminished specificity and higher incidence of hypersensitivity reaction to the antibody injections. When radiolabeled polyconal antibodies are used in imaging, they may go to sites of inflammation or infection, as well as a variety of nontargeted tumors and normal tissue. The advent of hybridoma technology enabled the production of the more specific monoclonal antibodies. However, monoclonal antibodies may also crossreact with antigens shared by other tumors, though less commonly than polyclonal. Compared to polyclonal, Mabs have a lower incidence of hypersensitivity reactions and HAMA production. Further advances in immunology have enabled the production of human or humanized Mab fragments and subfragments, which have practically eliminated these reactions.
Antibody engineering and its therapeutic applications
Published in International Reviews of Immunology, 2023
Divya Kandari, Rakesh Bhatnagar
Edward Jenner established the era of antibody (Ab) research when he first noted that injecting fluid of cowpox pustules into humans protects against smallpox.1 Next, Von Behring and Kitasato discovered the prophylactic and therapeutic functions of Abs in the nineteenth century, which marked the use of human and animal serums in medicine.2 Subsequently, in 1972, Gerald Edelman and Rodney Porter were awarded the Nobel Prize for their significant contributions to the knowledge of the Ab structure.1 In 1975, Köhler and Milstein published their landmark work demonstrating the fusion of Ab plasma and myeloma cells to form a hybridoma.3 Naturally, mAbs arise from single B cell clones, and they naturally protect the host organism from pathogens and target the infected cells. The unique nature of hybridoma cells is their ability to propagate indefinitely and, thus theoretically, to produce an unlimited amount of the Ab encoded by the parent B cell.4 The first monoclonal Ab (mAb) generated using this technology was reported in 1975 and licensed in 1986.4,5 The development of several high-quality mAbs then marked hybridoma technology as the core Ab technology.4
The potential role of opioid vaccines and monoclonal antibodies in the opioid overdose crisis
Published in Expert Opinion on Investigational Drugs, 2023
Suky Martinez, Hannah Harris, Thomas Chao, Rachel Luba, Marco Pravetoni, Sandra D Comer, Jermaine D Jones
Another immunotherapeutic approach to treating opioid overdose is passive immunization with monoclonal antibodies (mAbs) that target specific opioids. Like the antibodies that are produced through active immunization with a vaccine, mAbs bind and sequester opioid drug molecules in the serum and other organs, which prevents them from entering the central nervous system [15]. Monoclonal antibodies are primarily produced from antigen-specific B cell lymphocytes via several techniques including hybridoma technology, phage display, and cloning and expression of antibody binding domains as recombinant monoclonal antibodies [15]. One of the potential advantages of mAbs is their rapid onset of action and ability to bind opioids after a single administration [16]. Therefore, mAbs could be useful for reversing an acute opioid overdose. If the mAb is long-lasting, this approach also could prevent an opioid overdose. One recent study in rodents found that the administration of mAbs successfully reversed fentanyl-induced respiratory depression, antinociception, and bradycardia for up to a week [17]. Other rodent studies from independent groups also show the preclinical efficacy of anti-opioid mAbs and the viability of chimeric or humanized mAbs against opioids [15,16,18,19]. In sum, preclinical findings in these rodent models suggest that opioid vaccines and monoclonal antibodies have significant potential in the treatment of opioid overdose.
Antibody therapies for the treatment of acute myeloid leukemia: exploring current and emerging therapeutic targets
Published in Expert Opinion on Investigational Drugs, 2023
Joshua W. Morse, Margarita Rios, John Ye, Adan Rios, Cheng Cheng Zhang, Naval G. Daver, Courtney D. DiNardo, Ningyan Zhang, Zhiqiang An
The term bispecific antibody (bsAb) describes a large family of therapeutic molecules with two antigen recognition sites. The bsAbs used to target leukemias are typically immune cell engagers (ICEs) in which one antigen recognition site targets a leukemia-specific antigen (LSA) while the other targets an immune cell antigen (commonly CD3 on T cells), allowing for synchronous targeting and facilitating of host immunity in an MHC-independent manner [148]. Bispecific antibodies were first generated in the 1960s when antigen-binding fragments from two different polyclonal sera were re-associated into bispecific F(ab’)2 molecules. With the development of hybridoma technology in 1975 and antibody engineering in the last three decades, it is now possible to generate antibodies of more than one defined specificity with relative ease [149]. Generally, these are divided into two major classes: those lacking an Fc region (Non-IgG-Like) and those bearing an Fc region (IgG-Like) [150,151] (Fig. 4). De Gast et al. developed the first bsAb used in hematological malignancies, a bispecific T cell engager (BiTE) targeting CD3xCD19, without significant clinical response in non-Hodgkin lymphoma but with toxicities limited to grade II fever and chills following infusion [152]. Over 12 years later, the CD3xCD19 bsAb blinatumomab was approved by the FDA for second-line use in B-cell precursor ALL [153].