მონოკლონური ანტისხეულების (mAbs) გამოყენება და მათი სამომავლო პერსპექტივები
DOI:
https://doi.org/10.56580/GEOMEDI0001საკვანძო სიტყვები:
ანტისხეულები, მონოკლონური ანტისხეულები, mAbs, ანტიგენი, ცილა, დიაგნოსტიკა, COVID-19ანოტაცია
სტატიაში განხილულია მონოკლონური ანტისხეულების (mAbs) გამოყენების სფეროები და სამომავლო გამოყენების პერსპექტივები. თანამედროვე ეტაპზე მონოკლონური ანტისხეულების ეფექტურობა, სხვადასხვა ეტიოლოგიის დაავადებების საწინააღმდეგოდ, იძლევა იმისი ვარაუდის საფუძველს, რომ მომავალში კიდევ უფრო დაიხვეწება მონოკლონური ანტისხეულების მიღება, რაც ხელს შეუწყობს მათ ფართო გამოყენებას არა მარტო დაავადებების მკურნალობაში, არამედ დიაგნოსტიკაშიც.
მეტრიკები
წყაროები
MacDonald G, Primrose S, Biggins K, et al. Production and characterization of human-human and human-mouse hybridomas secreting Rh(D)-specific monoclonal antibodies. Scand J Immunol. 1987; 25(5): 477–483.
Ainai A, Kawase T, Ida A, et al. Renewal of EBV-hybridoma method: efficient generation of recombinant fully human neutralizing IgG antibodies specific for tetanus toxin by use of tetroma cells. Hum Antibodies. 2006; 15(4): 139–154.
Gram H, Strittmatter U, Lorenz M, Gluck D, Zenke G. Phage display as a rapid gene expression system: production of bioactive cytokinephage and generation of neutralizing monoclonal antibodies. J Immunol Methods. 1993; 161(2): 169–176.
Zhao XL, Yin J, Chen WQ, Jiang M, Yang G, Yang ZH. Generation and characterization of human monoclonal antibodies to G5, a linear neutralization epitope on glycoprotein of rabies virus, by phage display technology. Microbiol Immunol. 2008; 52(2): 89–93.
Jakobovits A. Production of fully human antibodies by transgenic mice. Curr Opin Biotechnol. 1995; 6(5): 561–566.
Jakobovits A, Green LL, Hardy MC, et al. Production of antigen-specific human antibodies from mice engineered with human heavy and light chain YACs. Ann N Y Acad Sci. 1995; 764: 525–535.
Osbourn J, Jermutus L, Duncan A. Current methods for the generation of human antibodies for the treatment of autoimmune diseases. Drug Discov Today. 2003; 8(18): 845–851.
Babcook JS, Leslie KB, Olsen OA, Salmon RA, Schrader JW. A novel strategy for generating monoclonal antibodies from single, isolated lymphocytes producing antibodies of defined specificities. Proc Natl Acad Sci U S A. 1996; 93(15): 7843–7848.
Ali M, Hitomi K, Nakano H. Generation of monoclonal antibodies using simplified single-cell reverse transcription-polymerase chain reaction and cell-free protein synthesis. J Biosci Bioeng. 2006; 101(3): 284–286.
Smith K, Garman L, Wrammert J, et al. Rapid generation of fully humanmonoclonal antibodies specific to a vaccinating antigen. Nat Protoc. 2009; 4(3): 372–384.
De StGroth SF, Scheidegger D. Production of monoclonal antibodies: strategy and tactics. J Immunol Methods. 1980; 35(1–2): 1–21.
Kennett RH. Hybridomas: a new dimension in biological analyses. In Vitro. 1981;17(12):1036–1050.
Steinitz M, Klein G. EBV-transformation of surface IgA-positive human lymphocytes. J Immunol. 1980; 125(1): 194–196.
Roome AJ, Reading CL. The use of Epstein-Barr virus transformation for the production of human monoclonal antibodies. Exp Biol. 1984; 43(1): 35–55.
Robinson JE, Holton D, Pacheco-Morell S, Liu J, McMurdo H. Identification of conserved and variant epitopes of human immunodeficiency virus type 1 (HIV-1) gp120 by human monoclonal antibodies produced by EBVtransformed cell lines. AIDS Res Hum Retroviruses. 1990; 6(5): 567–579.
Yamaura N, Makino M, Walsh LJ, Bruce AW, Choe BK. Production of monoclonal antibodies against prostatic acid phosphatase by in vitro immunization of human spleen cells. J Immunol Methods. 1985; 84(1–2):105–116.
Yu X, McGraw PA, House FS, Crowe JE Jr. An optimized electrofusionbased protocol for generating virus-specific human monoclonal antibodies. J Immunol Methods. 2008;336(2):142–151.
Yamashita M, Katakura Y, Shirahata S. Recent advances in the generation of human monoclonal antibody. Cytotechnology. 2007; 55(2–3): 55–60.
Lonberg N. Human antibodies from transgenic animals. Nat Biotechnol. 2005; 23(9): 1117–1125.
Lonberg N. Fully human antibodies from transgenic mouse and phage display platforms. Curr Opin Immunol. 2008; 20(4): 450–459.
Lonberg N. Human monoclonal antibodies from transgenic mice. Handb Exp Pharmacol. 2008; (181): 69–97.
Nelson AL, Dhimolea E, Reichert JM. Development trends for human monoclonal antibody therapeutics. Nat Rev Drug Discov. 2010; 9: 767–74.
Tyagi S, Sharma PK, Kumar N, Visht S. Hybridoma technique in pharmaceutical science. International Journal of Pharm Tech Research. 2011; 3(1): 459–463.
Zola, H. Monoclonal antibodies. In: Encyclopedia of Life Sciences. John Wiley & Sons: Chichester, UK; 2010: 1–9.
Edwards PA. Some properties and applications of monoclonal antibodies. Biochem J. 1981; 200(1): 1–10.
Ling NR. Properties of the monoclonal antibodies produced by hybridoma technology and their application to the study of diseases. Immunology. 1983; 49(1): 202–203.
Carter P. Improving the efficacy of antibody-based cancer therapies. Nat Rev Cancer. 2001; 1(2): 118–129.
Beckman RA, Weiner LM, Davis HM. Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors. Cancer. 2007; 109(2): 170–179.
Rang HP, Dale MM, Ritter JM, Flower RJ, Henderson G. Rang and Dale’s Pharmacology. Philadelphia, PA: Churchill Livingstone; 2003.
Waldmann TA. Immunotherapy: past, present and future. Nature Med. 2003; 9(3): 269–277.
Jacene HA, Filice R, Kasecamp W, Wahl RL. Comparison of 90Y-ibritumomab tiuxetan and 131I-to situ momab in clinical practice. J Nucl Med. 2007; 48(11): 1767–1776.
Jody Tucker Mack, Gemtuzumabozogamicin, xPharm: The Comprehensive Pharmacology Reference, 2007, Pages 1-7.
https://www.breastcancer.org/treatment/targeted_therapies/herceptin#effects
WHO Drug Information, Vol. 19, No. 4, 2005 Proposed INN List 94, p.333
Merck Index 14th Edition Monograph number 10585.
Ramakrishnan MS, Eswaraiah A, Crombet T, Piedra P, Saurez G, Iyer H, Arvind AS (2009). "Nimotuzumab, a promising therapeutic monoclonal for treatment of tumors of epithelial origin". mAbs. 1 (1): 41–8. doi:10.4161/mabs.1.1.7509. PMC 2715181. PMID 20046573.
Van Dyck, C. H. (2018) ‘Anti-Amyloid-β Monoclonal Antibodies for Alzheimer’s Disease: Pitfalls and Promise’, Biological Psychiatry. doi: 10.1016/j.biopsych.2017.08.010.
Xu X, Han M, Li T, Sun W, Wang D, Fu B, et al. Effective treatment of severe COVID-19 patients with tocilizumab. Proc Natl AcadSci USA. 2020; 117(20): 10970–5. https://doi.org/10.1073/pnas.2005615117
Guaraldi G, Meschiari M, Cozzi-Lepri A, Milic J, Tonelli R, Menozzi M, et al. Tocilizumab in patients with severe COVID-19: a retrospective cohort study. Lancet Rheumatol. 2020; 2(8): e474–e484. https://doi.org/10.1016/S2665-9913(20)30173-9
Fu B, Xu X, Wei H. Why tocilizumab could be an effective treatment for severe COVID-19? J Transl Med. 2020;18(1):164. https://doi.org/10.1186/s12967-020-02339-3
Zhang C, Wu Z, Li JW, Zhao H, Wang GQ. Cytokine release syndrome in severe COVID-19: interleukin-6 receptor antagonist tocilizumab may be the key to reduce mortality. Int J Antimicrob Agents. 2020;55(5):105954.
Zhou F, Yu T, Du R, Fan G, Liu Y, Liu Z, et al. Clinical course and risk factors for mortality of adult in patients with COVID-19 in Wuhan, China: a retrospective cohort study. Lancet. 2020; 395(10229): 1054– 62. https://doi.org/10.1016/S0140-6736(20)30566-3