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Review
. 2024 Nov 11;13(4):90.
doi: 10.3390/antib13040090.

A Brief Chronicle of Antibody Research and Technological Advances

Affiliations
Review

A Brief Chronicle of Antibody Research and Technological Advances

Kazutaka Araki et al. Antibodies (Basel). .

Abstract

This review briefly traces the historical development of antibody research and related technologies. The path from early perceptions of immunity to the emergence of modern immunotherapy has been marked by pivotal discoveries and technological advances. Early insights into immunity led to the development of vaccination and serotherapy. The elucidation of antibody structure and function paved the way for monoclonal antibody technology and its application in diagnosis and therapy. Breakthroughs in genetic engineering have enabled the production of humanized antibodies and the advances in Fc engineering, thereby increasing therapeutic efficacy. The discovery of immune checkpoints and cytokines revolutionized the treatment of cancer and autoimmune diseases. The field continues to evolve rapidly with the advent of antibody-drug conjugates, bispecific antibodies, and CAR T-cell therapies. As we face global health challenges, antibody research remains at the forefront of medical innovation and offers promising solutions for the future.

Keywords: antibody; immunoglobulin; immunology.

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Conflict of interest statement

Author Ryota Maeda is employed by COGNANO Inc. and participated in the research as a co-author. Author Kazutaka Araki declares no commercial or financial relationships that could constitute potential conflicts of interest.

Figures

Figure 4
Figure 4
Timeline of selected achievements or events from 1961 to 1980. References in this timeline include works by Chodirker & Tomasi [73], Ceppellini et al. [74], Möller [75], Cooper et al. [8], Ishizaka et al. [76], Edelman et al. [5], Wang et al. [77], Wu & Kabat [78], Laemmli [79], Engvall & Perlmann [80], Van Weemen & Schuurs [81], Aviv & Leder [82], Julius et al. [83], Jackson et al. [84], Cohen et al. [85], Tonegawa et al. [86], Köhler & Milstein [9], Hozumi & Tonegawa [87], Maxam & Gilbert [88], Silverton et al. [89], Sanger et al. [90], Itakura et al. [91], Hutchison et al. [92], Towbin et al. [93], and Renart et al. [94].
Figure 1
Figure 1
Crystal structure and schematic diagram of immunoglobulin G. The crystal structure of immunoglobulin G1 (PDB code: 1IGY) is illustrated using a ribbon model on the left and a schematic diagram on the right [12]. The light variable (VL), light constant (CL), heavy variable (VH), and heavy constant (CH) regions are depicted in light red, dark red, light blue, and dark blue, respectively. Carbohydrate residues attached to the Fc region are shown in green using stick models.
Figure 2
Figure 2
Timeline of selected achievements or events from the 18th century to the early 20th century. References in this timeline include works by Timonius & Woodward [14], Pylarini [15], Jenner [16], Jones [17], Haeckel [18], Metchnikoff [19], Behring [20], Ehrlich [21,22], Deutsch [23], Landsteiner [24], Portier [25], and Von [26].
Figure 3
Figure 3
Timeline of selected achievements or events from 1921 to 1960. References in this timeline include works by Avery & Heidelberger [44], Svedberg [45], Heidelberger & Kendall [46], Heidelberger & Pedersen [47], Tiselius [48], Coons et al. [49], Bjørneboe & Gormsen [50], Coombs et al. [51], Fagraeus [6], Billingham et al. [52], Jerne [53], Puck et al. [54], Nossal & Lederberg [55], Edelman [56], Burnet [7], Heremans et al. [57], and Yalow & Berson [58].
Figure 5
Figure 5
Comparison of immunoglobulin isotypes: structure and function. This diagram shows the five main classes of immunoglobulins, each with a specific role in the immune system. All immunoglobulins have a basic structure that is made up of two heavy chains and two light chains arranged in a Y shape. The type of heavy chain is called the isotype, and it determines the antibody’s class and its specific function. The Fc region of the antibody molecule, found at the base of the Y shape, is essential for activities such as opsonization (labeling pathogens for destruction), complement activation (a sequence of proteins that helps eliminate pathogens), and binding to various cell receptors. The variable region at the tips of the Y shape is responsible for recognizing and binding to specific antigens or foreign substances. The five classes of immunoglobulins—IgG, IgM, IgA, IgD, and IgE—each have distinct characteristics in terms of structure, function, and expression, as briefly described in the topics section.
Figure 6
Figure 6
Timeline of selected achievements or events from 1981 to 2000. References in this timeline include works by Alt et al. [149], Miller et al. [150], Tonegawa [10], Morrison et al. [151], Boulianne et al. [152], Smith [153], Jones et al. [11], Better et al. [154], Hale et al. [155], Schatz et al. [156], Scott & Smith [157], McCafferty et al. [158], Ishida et al. [159], Elliott et al. [160], Leach et al. [161], and Muramatsu et al. [148].
Figure 7
Figure 7
Timeline of selected achievements or events from 2001.

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