Plant-Produced Therapeutic Crizanlizumab Monoclonal Antibody Binds P-Selectin to Alleviate Vaso-occlusive Pain Crises in Sickle Cell Disease.
Crizanlizumab
P-Selectin
Sickle cell disease
Transgenic plant
Journal
Molecular biotechnology
ISSN: 1559-0305
Titre abrégé: Mol Biotechnol
Pays: Switzerland
ID NLM: 9423533
Informations de publication
Date de publication:
15 Mar 2024
15 Mar 2024
Historique:
received:
20
09
2023
accepted:
02
02
2024
medline:
16
3
2024
pubmed:
16
3
2024
entrez:
16
3
2024
Statut:
aheadofprint
Résumé
Sickle Cell Disease (SCD) is a severe genetic disorder causing vascular occlusion and pain by upregulating the adhesion molecule P-selectin on endothelial cells and platelets. It primarily affects infants and children, causing chronic pain, circulatory problems, organ damage, and complications. Thus, effective treatment and management are crucial to reduce SCD-related risks. Anti-P-selectin antibody Crizanlizumab (Crimab) has been used to treat SCD. In this study, the heavy and light chain (HC and LC) genes of anti-P-Selectin antibody Crimab were cloned into a plant expression binary vector. The HC gene was under control of the duplicated 35S promoter and nopaline synthase (NOS) terminator, whereas the LC gene was under control of the potato proteinase inhibitor II (PIN2) promoter and PIN2 terminator. Agrobacterium tumefaciens LBA4404 was used to transfer the genes into the tobacco (Nicotiana tabacum cv. Xanthi) plant. In plants the genomic PCR and western blot confirmed gene presence and expression of HC and LC Crimab proteins in the plant, respectively. Crimab was successfully purified from transgenic plant leaf using protein A affinity chromatography. In ELISA, plant-derived Crimab (Crimab
Identifiants
pubmed: 38491245
doi: 10.1007/s12033-024-01110-z
pii: 10.1007/s12033-024-01110-z
doi:
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Lim, C. Y., Park, S. R., Lee, J. H., & Ko, K. (2015). Purification of anti-colorectal cancer monoclonal antibody CO17-1A from insect cell culture using a French press and sonication. Entomological Research, 45, 102–109.
doi: 10.1111/1748-5967.12100
Brodsky, J. L., & Skach, W. R. (2011). Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems. Current Opinion in Cell Biology, 23, 464–475.
doi: 10.1016/j.ceb.2011.05.004
pubmed: 21664808
pmcid: 3154734
Dobrica, M. O., Lazar, C., Paruch, L., Skomedal, H., Steen, H., Haugslien, S., Tucureanu, C., Caras, I., Onu, A., & Ciulean, S. (2017). A novel chimeric Hepatitis B virus S/preS1 antigen produced in mammalian and plant cells elicits stronger humoral and cellular immune response than the standard vaccine-constituent, S protein. Antiviral Research, 144, 256–265.
doi: 10.1016/j.antiviral.2017.06.017
pubmed: 28666757
Twyman, R., Schillberg, S., & Fischer, R. (2012). The production of vaccines and therapeutic antibodies in plants. In A. Wang & S. Ma (Eds.), Molecular farming in plants: Recent advances and future prospects. Springer.
Dubey, K. K., Luke, G. A., Knox, C., Kumar, P., Pletschke, B. I., Singh, P. K., & Shukla, P. (2018). Vaccine and antibody production in plants: Developments and computational tools. Briefings in Functional Genomics, 17, 295–307.
doi: 10.1093/bfgp/ely020
pubmed: 29982427
Faye, L., & Gomord, V. (2010). Success stories in molecular farming—a brief overview. Plant Biotechnology Journal, 8, 525–528.
doi: 10.1111/j.1467-7652.2010.00521.x
pubmed: 20500680
Gupta, S. K., & Shukla, P. (2017). Microbial platform technology for recombinant antibody fragment production: A review. Critical Reviews in Microbiology, 43, 31–42.
doi: 10.3109/1040841X.2016.1150959
pubmed: 27387055
Kang, Y. J., Kim, D. S., Kim, S., Seo, Y. J., & Ko, K. (2023). Plant-derived PAP proteins fused to immunoglobulin A and M Fc domains induce anti-prostate cancer immune response in mice. BMB Reports, 56, 392–397.
doi: 10.5483/BMBRep.2022-0207
pubmed: 37037672
pmcid: 10390288
Park, S. R., Lee, J. H., Kim, K., Kim, T. M., Lee, S. H., Choo, Y. K., Kim, K. S., & Ko, K. (2020). Expression and in vitro function of anti-breast cancer llama-based single domain antibody VHH expressed in tobacco plants. International Journal of Molecular Sciences, 21, 1354.
doi: 10.3390/ijms21041354
pubmed: 32079309
pmcid: 7072948
Kim, K., Kang, Y. J., Park, S. R., Kim, D. S., Lee, S. W., Ko, K., Ponndorf, D., & Ko, K. (2021). Effect of leaf position and days post-infiltration on transient expression of colorectal cancer vaccine candidate proteins GA733-Fc and GA733-FcK in Nicotiana benthamiana plant. PeerJ, 9, e10851.
doi: 10.7717/peerj.10851
pubmed: 33868796
pmcid: 8035899
Lim, S., Kim, D. S., & Ko, K. (2020). Expression of a large single-chain 13F6 antibody with binding activity against Ebola virus-like particles in a plant system. International Journal of Molecular Sciences, 21, 7007.
doi: 10.3390/ijms21197007
pubmed: 32977599
pmcid: 7582593
Shin, C., Kim, K., Kang, Y. J., Kim, D. S., Seo, Y. J., Park, S. R., Kim, M. K., Lee, Y. K., Kim, D., & Ko, K. S. (2022). Effect of IgG Fc-fusion and KDEL-ER retention signal on prostate-specific antigen expression in plant and its immune in mice. Plant Biotechnology Reports, 16, 729–740.
doi: 10.1007/s11816-022-00810-9
Kang, Y. J., Lee, S. S., & Kim, S. G. (2023). Intraoral approach for the treatment of non-infiltrating angiolipoma of the floor of the mouth in an elderly patient: A case report with review of the literature. Experimental and Therapeutic Medicine, 26, 458.
doi: 10.3892/etm.2023.12157
pubmed: 37614439
pmcid: 10443065
Oh, S., Kim, K., Kang, Y. J., Hwang, H., Kim, Y., Hinterdorfer, P., Kim, M. K., Ko, K., Lee, Y. K., Kim, D., Myung, S. C., & Ko, K. S. (2023). Co-transient expression of PSA-Fc and PAP-Fc fusion protein in plant as prostate cancer vaccine candidates and immune responses in mice. Plant Cell Reports, 42, 1203–1215.
doi: 10.1007/s00299-023-03028-3
pubmed: 37269373
Lim, C. Y., Kim, D. S., Kang, Y., Lee, Y. R., Kim, K., Kim, D. S., Kim, M. S., & Ko, K. (2022). Immune responses to plant-derived recombinant colorectal cancer glycoprotein EpCAM-FcK fusion protein in mice. Biomolecules & Therapeutics (Seoul), 30, 546–552.
doi: 10.4062/biomolther.2022.103
Moshi, G., Sheehan, V. A., & Makani, J. (2022). Africa must participate in finding a gene therapy cure for sickle-cell disease. Nature Medicine, 28, 2451–2452.
doi: 10.1038/s41591-022-02033-5
pubmed: 36203001
Karki, N. R., Saunders, K., & Kutlar, A. (2022). A critical evaluation of crizanlizumab for the treatment of sickle cell disease. Expert Review of Hematology, 15, 5–13.
doi: 10.1080/17474086.2022.2023007
pubmed: 34942078
Ataga, K. I., Kutlar, A., Kanter, J., Liles, D., Cancado, R., Friedrisch, J., Guthrie, T. H., Knight-Madden, J., Alvarez, O. A., Gordeuk, V. R., Gualandro, S., Colella, M. P., Smith, W. R., Rollins, S. A., Stocker, J. W., & Rother, R. P. (2017). Crizanlizumab for the prevention of pain crises in sickle cell disease. New England Journal of Medicine, 376, 429–439.
doi: 10.1056/NEJMoa1611770
pubmed: 27959701
Frenette, P. S., Denis, C. V., Weiss, L., Jurk, K., Subbarao, S., Kehrel, B., Hartwig, J. H., Vestweber, D., & Wagner, D. D. (2000). P-selectin glycoprotein ligand 1 (PSGL-1) is expressed on platelets and can mediate platelet-endothelial interactions in vivo. Journal of Experimental Medicine, 191, 1413–1422.
doi: 10.1084/jem.191.8.1413
pubmed: 10770806
pmcid: 2193129
Kaur, K., Kennedy, K., & Liles, D. (2023). Crizanlizumab in sickle cell disease. Pain Management, 13, 603–612.
doi: 10.2217/pmt-2023-0031
Afana, M. S., Abu-Tineh, M., Alshurafa, A., Yasin, A. K., Ahmed, K., Abdulgayoom, M., & Yassin, M. A. (2023). Recurrence of acute chest syndrome post stopping Crizanlizumab, the dilemma of stopping vs continuation in patient with sickle cell disease: Case report. Hematology, 28, 2229115.
doi: 10.1080/16078454.2023.2229115
pubmed: 37519115
Kay, R., Chan, A., Daly, M., & McPherson, J. (1987). Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes. Science, 236, 1299–1302.
doi: 10.1126/science.236.4806.1299
pubmed: 17770331
Lee, C. E., Lee, J. H., Chung, H. J., Lee, D. W., Lim, J. S., Kim, K., Kim, J. W., Lee, Y. S., Kim, K. S., Min, H. J., Ko, K., & Myung, S. C. (2023). Expression and in vitro function of anti-PD-L1 human antibody expressed in plant. Plant Biotechnology Reports, 17, 531–539.
doi: 10.1007/s11816-023-00844-7
Castilho, A., & Steinkellner, H. (2012). Glyco-engineering in plants to produce human-like N-glycan structures. Biotechnology Journal, 7, 1088.
doi: 10.1002/biot.201200032
pubmed: 22890723
Alamillo, J. M., Monger, W., Sola, I., Garcia, B., Perrin, Y., Bestagno, M., Burrone, O. R., Sabella, P., Plana-Duran, J., Enjuanes, L., Lomonossoff, G. P., & Garcia, J. A. (2006). Use of virus vectors for the expression in plants of active full-length and single chain anti-coronavirus antibodies. Biotechnology Journal, 1, 1103–1111.
doi: 10.1002/biot.200600143
pubmed: 17004304
pmcid: 7161777
Lee, Y. R., Lim, C. Y., Lim, S., Park, S. R., Hong, J. P., Kim, J., Lee, H. E., Ko, K., & Kim, D. S. (2020). Expression of colorectal cancer antigenic protein fused to IgM Fc in Chinese cabbage (Brassica rapa). Plants (Basel), 9, 1466.
doi: 10.3390/plants9111466
pubmed: 33143243
Kim, D. S., Song, I., & Ko, K. (2018). Low risk of pollen-mediated gene flow in transgenic plants under greenhouse conditions. Horticulture, Environment and Biotechnology, 59, 723–728.
doi: 10.1007/s13580-018-0074-3
Kang, Y. J., Kim, D. S., Myung, S. C., & Ko, K. (2017). Expression of a human prostatic acid phosphatase (PAP)-IgM Fc fusion protein in plants using tissue subculture. Frontiers in Plant Science, 8, 274.
doi: 10.3389/fpls.2017.00274
pubmed: 28293250
pmcid: 5329016