MONOCLONAL ANTIBODIES: FROM HYBRIDOMA TECHNOLOGY TO NEXT – GENERATION THERAPEUTIC INNOVATIONS.
Abstract
Immunoglobulin derivatives which are derived from the monoclonal cell line and which offers a wide range of specificity are the monoclonal antibodies. They are specially produced by the hybridoma technology by the fusion of B-cells with the immortal myeloma cells in presence of PEG. Humanized mAbs are considered to be the fastest growing group in clinical trials. After development, these mAbs undergoes analytical evaluation for their efficient characterization. Developed hybridomas can be preserved for long term use through the cryopreservation techniques. Monoclonal antibodies can be delivered for the therapeutic purpose through the various systemic and non-systemic routes. Large groups of the antibodies are found to be very effective through the oral routes and the ophthalmic routes. Besides the therapeutic application for the treatment of various infectious and autoimmune diseases, these groups of therapeutics show different limitations. Monoclonal antibodies after development suffers from the stability issues and using the various techniques, the stability can be increased. With the advancement of science and technology, we can observe various advances in the monoclonal antibody development like brain targeting is possible through the antibody engineering techniques. Variability and control challenges in the serum based acquisitions, consumption of time, difficulty in the development, potential limitation in the sequence and epitope diversity etc. are some of the challenges associated with the monoclonal antibodies
Keywords:
Immunoglobulin, Hybridoma Technology, Cryopreservation, Antibody Engineering
References
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33. Dara SR. An Overview of the Use of Natural Indicators in Acid-Base Titrations. UPI Journal of Pharmaceutical, Medical and Health Sciences. 2024 Jul 23:29-35.
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2. Pelletier JP, Mukhtar F. Passive monoclonal and polyclonal antibody therapies. In: Fung MK, Eder AF, Spitalnik SL, Westhoff CM, editors. Immunologic Concepts in Transfusion Medicine. Amsterdam: Elsevier; 2020. p. 251-348. doi:10.1016/B978-0-323-67509-3.00016-0.
3. Jahanshahlu L, Rezaei N. Monoclonal antibody as a potential anti-COVID-19. Biomed Pharmacother. 2020;129:110337. doi:10.1016/j.biopha.2020.110337.
4. Shepard HM, Phillips GL, Thanos CD, Feldmann M. Developments in therapy with monoclonal antibodies and related proteins. Clin Med (Lond). 2017;17(3):220-232. doi:10.7861/clinmedicine.17-3-220.
5. Manso T, Kushwaha A, Abdollahi N, Duroux P, Giudicelli V, Kossida S. Mechanisms of action of monoclonal antibodies in oncology integrated in IMGT/mAb-DB. Front Immunol. 2023;14:1129323. doi:10.3389/fimmu.2023.1129323.
6. Moorthy BS, Xie B, Moussa EM, Iyer LK, Chandrasekhar S, Panchal JP, et al. Structure of monoclonal antibodies. In: Biobetters: Protein Engineering to Approach the Curative. New York: Springer; 2015. p. 81-89.
7. Nap M, Hammarström ML, Börmer O, Hammarström S, Wagener C, Handt S, et al. Specificity and affinity of monoclonal antibodies against carcinoembryonic antigen. Cancer Res. 1992;52(8):2329-2339.
8. Nap M, Hammarström ML, Börmer O, Hammarström S, Wagener C, Handt S, et al. Specificity and affinity of monoclonal antibodies against carcinoembryonic antigen. Cancer Res. 1992;52(8):2329-2339. (Duplicate of Reference 7; retain only one in final bibliography.)
9. Köhler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975;256(5517):495-497.
10. Morrison SL, Johnson MJ, Herzenberg LA, Oi VT. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc Natl Acad Sci U S A. 1984;81(21):6851-6855.
11. Jones PT, Dear PH, Foote J, Neuberger MS, Winter G. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature. 1986;321(6069):522-525.
12. Weiner LM, Surana R, Wang S. Monoclonal antibodies: versatile platforms for cancer immunotherapy. Nat Rev Immunol. 2010;10(5):317-327.
13. Hamers-Casterman CT, Atarhouch T, Muyldermans SA, Robinson G, Hammers C, Songa EB, et al. Naturally occurring antibodies devoid of light chains. Nature. 1993;363(6428):446-448.
14. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P. Isolating, cloning, and sequencing DNA. In: Molecular Biology of the Cell. 4th ed. New York: Garland Science; 2002.
15. Kothari M, Wanjari A, Acharya S, Karwa V, Chavhan R, Kumar S, et al. A comprehensive review of monoclonal antibodies in modern medicine: tracing the evolution of a revolutionary therapeutic approach. Cureus. 2024;16(6):e62006. (Verify article number from original source.)
16. Kothari M, Wanjari A, Acharya S, Karwa V, Chavhan R, Kumar S, et al. A comprehensive review of monoclonal antibodies in modern medicine: tracing the evolution of a revolutionary therapeutic approach. Cureus. 2024;16(6). (Duplicate of Reference 15; retain only one.)
17. Yingngam B. Monoclonal antibody. In: Critical Developments in Cancer Immunotherapy. 2024. p. 419.
18. Fekete S, Gassner AL, Rudaz S, Schappler J, Guillarme D. Analytical strategies for the characterization of therapeutic monoclonal antibodies. TrAC Trends Anal Chem. 2013;42:74-83. doi:10.1016/j.trac.2012.09.012.
19. Fan G, Wang Z, Hao M, Li J. Bispecific antibodies and their applications. J Hematol Oncol. 2015;8(1):130.
20. Fan G, Wang Z, Hao M, Li J. Bispecific antibodies and their applications. J Hematol Oncol. 2015;8(1):130. doi:10.1186/s13045-015-0227-0. (Duplicate of Reference 19.)
21. Tapia-Galisteo A, Compte M, Álvarez-Vallina L, Sanz L. When three is not a crowd: trispecific antibodies for enhanced cancer immunotherapy. Theranostics. 2023;13(3):1028-1048. doi:10.7150/thno.81494.
22. Zhao D, Chen J, Hu X, Zhang S. Catalytic antibodies: design, expression, and their applications in medicine. Appl Biochem Biotechnol. 2023;195(2):1514-1540. doi:10.1007/s12010-022-04183-1.
23. Hamers-Casterman CT, Atarhouch T, Muyldermans SA, Robinson G, Hammers C, Songa EB, et al. Naturally occurring antibodies devoid of light chains. Nature. 1993;363(6428):446-448. doi:10.1038/363446a0. (Duplicate of Reference 13.)
24. Ingram JR, Schmidt FI, Ploegh HL. Exploiting nanobodies' singular traits. Annu Rev Immunol. 2018;36:695-715. doi:10.1146/annurev-immunol-042617-053327.
25. Zhang A, Stacey HD, D'Agostino MR, Tugg Y, Marzok A, Miller MS. Beyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection. Nat Rev Immunol. 2023;23(6):381-396. doi:10.1038/s41577-022-00813-1.
26. Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol. 2007;25:21-50. doi:10.1146/annurev.immunol.25.022106.141702.
27. Abdeldaim DT, Schindowski K. Fc-engineered therapeutic antibodies: recent advances and future directions. Pharmaceutics. 2023;15(10):2402. doi:10.3390/pharmaceutics15102402.
28. Rao C. Evaluation of Antiulcer Activity of Picrasma Quassioides Bennett Aqueous Extract in Rodents. Vedic Research International Phytomedicine. 2013 Jan 1.
29. Gindi S, Methra T, Chandu BR, Boyina R, Dasari V. Antiurolithiatic and invitro anti-oxidant activity of leaves of Ageratum conyzoides in rat. World J. Pharm. Pharm. Sci. 2013 Feb 8;2:636-49.
30. Nama S, Chandu BR, Awen BZ, Khagga M. Development and validation of a new RP-HPLC method for the determination of aprepitant in solid dosage forms. Trop J Pharm Res. 2011;10(4):489-494.
31. Kiranmai M, Renuka P, Brahmaiah B, Chandu BR. Vitamin D as a promising anticancer agent. Int J Res Pharm Chem. 2012;2(2):636-649.
32. Kundeti K. A Review on: Pharmacokinetic and Drug Disposition. Journal of Case Studies and Case Reports. 2023 Aug 31:10-5.
33. Dara SR. An Overview of the Use of Natural Indicators in Acid-Base Titrations. UPI Journal of Pharmaceutical, Medical and Health Sciences. 2024 Jul 23:29-35.
34. Adiki SK, Lahari K, Dey B, Khalf AM, Al-Sharif SM, Diaf SR, Katakam P, Chandu BR. Validated UV Method Development for the Simultaneous Estimation of Rabeprazole sodium and Cinitapride in Tablets.
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11/05/2026
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Paidimala, B. (2026). MONOCLONAL ANTIBODIES: FROM HYBRIDOMA TECHNOLOGY TO NEXT – GENERATION THERAPEUTIC INNOVATIONS. The Journal of Multidisciplinary Research, 6(1), 18-23. Retrieved from https://saapjournals.org/index.php/tjmdr/article/view/887
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