综述 |
|
|
|
|
不同表达系统的治疗性纳米抗体研究进展 |
孙白荷1,2,吴悦1,2,赵芮3,楼雨馨2,李婉婷2,李延飞2,*(),马琳琳2,*() |
1 上海理工大学健康科学与工程学院 上海 200093 2 上海健康医学院医学技术学院 上海 201318 3 上海市东海老年护理医院 上海 201303 |
|
Research Progress of Therapeutic Nanobodies with Different Expression Systems |
SUN Bai-he1,2,WU Yue1,2,ZHAO Rui3,LOU Yu-xin2,LI Wan-ting2,LI Yan-fei2,*(),MA Lin-lin2,*() |
1 School of Health Science and Engineering,University of Shanghai for Science and Technology,Shanghai 200093,China 2 School of Medical Technology,Shanghai University of Medicine & Health Sciences,Shanghai 201318,China 3 Shanghai Donghai Geriatric Nursing Hospital,Shanghai 201303,China |
引用本文:
孙白荷, 吴悦, 赵芮, 楼雨馨, 李婉婷, 李延飞, 马琳琳. 不同表达系统的治疗性纳米抗体研究进展[J]. 中国生物工程杂志, 2023, 43(11): 43-55.
SUN Bai-he, WU Yue, ZHAO Rui, LOU Yu-xin, LI Wan-ting, LI Yan-fei, MA Lin-lin. Research Progress of Therapeutic Nanobodies with Different Expression Systems. China Biotechnology, 2023, 43(11): 43-55.
链接本文:
https://manu60.magtech.com.cn/biotech/CN/10.13523/j.cb.2305026
或
https://manu60.magtech.com.cn/biotech/CN/Y2023/V43/I11/43
|
[1] |
Tillib S V. “Camel nanoantibody” is an efficient tool for research, diagnostics and therapy. Molecular Biology, 2011, 45(1): 66-73.
doi: 10.1134/S0026893311010134
|
[2] |
Huang L, Gainkam L O T, Caveliers V, et al. SPECT imaging with 99mTc-labeled EGFR-specific nanobody for in vivo monitoring of EGFR expression. Molecular Imaging and Biology, 2008, 10(3): 167-175.
doi: 10.1007/s11307-008-0133-8
|
[3] |
Kenanova V, Wu A M. Tailoring antibodies for radionuclide delivery. Expert Opinion on Drug Delivery, 2006, 3(1): 53-70.
pmid: 16370940
|
[4] |
Mordenti J. Comparisons of the intraocular tissue distribution, pharmacokinetics, and safety of 125I-labeled full-length and fab antibodies in Rhesus monkeys following intravitreal administration. Toxicologic Pathology, 1999, 27(5): 536-544.
doi: 10.1177/019262339902700507
pmid: 10528633
|
[5] |
Van de Wiele C, Revets H, Mertens N. Radioimmunoimaging. Advances and prospects. Nuclear Medicine and Molecular Imaging, 2004, 48(4): 317-325.
doi: 10.1007/s13139-014-0294-0
|
[6] |
Vaneycken I, D’huyvetter M, Hernot S, et al. Immuno-imaging using nanobodies. Current Opinion in Biotechnology, 2011, 22(6): 877-881.
doi: 10.1016/j.copbio.2011.06.009
pmid: 21726996
|
[7] |
Hamers-Casterman C, Atarhouch T, Muyldermans S, et al. Naturally occurring antibodies devoid of light chains. Nature, 1993, 363(6428): 446-448.
doi: 10.1038/363446a0
|
[8] |
Muyldermans S. Nanobodies: natural single-domain antibodies. Annual Review of Biochemistry, 2013, 82: 775-797.
doi: 10.1146/annurev-biochem-063011-092449
pmid: 23495938
|
[9] |
Bathula N V, Bommadevara H, Hayes J M. Nanobodies: the future of antibody-based immune therapeutics. Cancer Biotherapy & Radiopharmaceuticals, 2021, 36(2): 109-122.
|
[10] |
Farajpour Z, Rahbarizadeh F, Kazemi B, et al. A nanobody directed to a functional epitope on VEGF, as a novel strategy for cancer treatment. Biochemical and Biophysical Research Communications, 2014, 446(1): 132-136.
doi: 10.1016/j.bbrc.2014.02.069
pmid: 24569074
|
[11] |
Li T, Bourgeois J P, Celli S, et al. Cell-penetrating anti-GFAP VHH and corresponding fluorescent fusion protein VHH-GFP spontaneously cross the blood-brain barrier and specifically recognize astrocytes: application to brain imaging. FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology, 2012, 26(10): 3969-3979.
doi: 10.1096/fsb2.v26.10
|
[12] |
Ren J, Zhang C, Ji F L, et al. Characterization and comparison of two peptide-tag specific nanobodies for immunoaffinity chromatography. Journal of Chromatography A, 2020, 1624: 461227.
doi: 10.1016/j.chroma.2020.461227
|
[13] |
Coppieters K, Dreier T, Silence K, et al. Formatted anti-tumor necrosis factor alpha VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen-induced arthritis. Arthritis and Rheumatism, 2006, 54(6): 1856-1866.
pmid: 16736523
|
[14] |
原博, 王杰文, 康广博, 等. 双特异性纳米抗体的研究进展及其应用. 中国生物工程杂志, 2021, 41(S1): 78-88.
|
|
Yuan B, Wang J W, Kang G B, et al. Research progress and application of bispecific nanobody. China Biotechnology, 2021, 41(S1): 78-88.
|
[15] |
van der Linden R H, Frenken L G, de Geus B, et al. Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies. Biochimica et Biophysica Acta, 1999, 1431(1): 37-46.
doi: 10.1016/s0167-4838(99)00030-8
pmid: 10209277
|
[16] |
Rossotti M A, Bélanger K, Henry K A, et al. Immunogenicity and humanization of single-domain antibodies. The FEBS Journal, 2022, 289(14): 4304-4327.
doi: 10.1111/febs.v289.14
|
[17] |
Akhila M V, Ken S N, Narwani Tarun J, et al. Discrete analysis of camelid variable domains: sequences, structures, and in-silico structure prediction. PeerJ, 2020, 8: e8408.
doi: 10.7717/peerj.8408
|
[18] |
Rathore A, Weiskopf A, Reason A. Defining critical quality attributes for monoclonal antibody therapeutic products. Biopharm International, 2014, 27(7): 34-36, 38.
|
[19] |
Cymer F, Beck H, Rohde A, et al. Therapeutic monoclonal antibody N-glycosylation: structure, function and therapeutic potential. Biologicals, 2018, 52: 1-11.
doi: 10.1016/j.biologicals.2017.11.001
|
[20] |
Habib I, Smolarek D, Hattab C, et al. VHH (nanobody) directed against human glycophorin A: a tool for autologous red cell agglutination assays. Analytical Biochemistry, 2013, 438(1): 82-89.
doi: 10.1016/j.ab.2013.03.020
|
[21] |
Fleetwood F, Devoogdt N, Pellis M, et al. Surface display of a single-domain antibody library on Gram-positive bacteria. Cellular and Molecular Life Sciences, 2013, 70(6): 1081-1093.
doi: 10.1007/s00018-012-1179-y
pmid: 23064703
|
[22] |
Ryckaert S, Pardon E, Steyaert J, et al. Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. Journal of Biotechnology, 2010, 145(2): 93-98.
doi: 10.1016/j.jbiotec.2009.10.010
pmid: 19861136
|
[23] |
Arbabi-Ghahroudi M, Tanha J, MacKenzie R. Prokaryotic expression of antibodies. Cancer and Metastasis Reviews, 2005, 24(4): 501-519.
doi: 10.1007/s10555-005-6193-1
pmid: 16408159
|
[24] |
Ventola C L. Progress in nanomedicine: approved and investigational nanodrugs. P & T: a Peer-Reviewed Journal for Formulary Management, 2017, 42(12): 742-755.
|
[25] |
Dmitriev O Y, Svetlana L, Serge M. Nanobodies as probes for protein dynamics in vitro and in cells. The Journal of Biological Chemistry, 2016, 291(8): 3767-3775.
doi: 10.1074/jbc.R115.679811
|
[26] |
Frenken L G J, van der Linden R H J, Hermans P W J J, et al. Isolation of antigen specific Llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae. Journal of Biotechnology, 2000, 78(1): 11-21.
doi: 10.1016/s0168-1656(99)00228-x
pmid: 10702907
|
[27] |
Liu Y K, Huang H. Expression of single-domain antibody in different systems. Applied Microbiology and Biotechnology, 2018, 102(2): 539-551.
doi: 10.1007/s00253-017-8644-3
pmid: 29177623
|
[28] |
Baeshen M N, Al-Hejin A M, Bora R S, et al. Production of biopharmaceuticals in E. coli: current scenario and future perspectives. Journal of Microbiology and Biotechnology, 2015, 25(7): 953-962.
doi: 10.4014/jmb.1412.12079
|
[29] |
Chao S Y, Liu Y H, Ding N, et al. Highly expressed soluble recombinant anti-GFP VHHs in Escherichia coli via optimized signal peptides, strains, and inducers. Frontiers in Molecular Biosciences, 2022, 9: 848829.
doi: 10.3389/fmolb.2022.848829
|
[30] |
Bakherad H, Gargari S L M, Rasooli I, et al. In vivo neutralization of botulinum neurotoxins serotype E with heavy-chain camelid antibodies (VHH). Molecular Biotechnology, 2013, 55(2): 159-167.
doi: 10.1007/s12033-013-9669-1
pmid: 23666874
|
[31] |
Shriver-Lake L C, Goldman E R, Zabetakis D, et al. Improved production of single domain antibodies with two disulfide bonds by co-expression of chaperone proteins in the Escherichia coli periplasm. Journal of Immunological Methods, 2017, 443: 64-67.
doi: S0022-1759(16)30321-0
pmid: 28131818
|
[32] |
Lao Z T, Li S Q, Liang J H, et al. Production and characterization of GPC3-N protein and its nanobody. Protein Expression and Purification, 2022, 195-196: 106094.
|
[33] |
Manta B, Boyd D, Berkmen M. Disulfide bond formation in the periplasm of Escherichia coli. EcoSal Plus, 2019, 8(2): ESP-0012-2018.
|
[34] |
de Marco A. Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. Microbial Cell Factories, 2009, 8: 26.
doi: 10.1186/1475-2859-8-26
pmid: 19442264
|
[35] |
Cornelis P. Expressing genes in different Escherichia coli compartments. Current Opinion in Biotechnology, 2000, 11(5): 450-454.
pmid: 11024362
|
[36] |
Shokri A, Sandén A, Larsson G. Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli. Applied Microbiology and Biotechnology, 2003, 60(6): 654-664.
pmid: 12664143
|
[37] |
Duggan S. Caplacizumab: first global approval. Drugs, 2018, 78(15): 1639-1642.
doi: 10.1007/s40265-018-0989-0
pmid: 30298461
|
[38] |
Takeuchi T, Kawanishi M, Nakanishi M, et al. Phase II/III results of a trial of anti-tumor necrosis factor multivalent NANOBODY compound ozoralizumab in patients with rheumatoid arthritis. Arthritis & Rheumatology, 2022, 74(11): 1776-1785.
|
[39] |
Luo D, Wen C X, Zhao R C, et al. High level expression and purification of recombinant proteins from Escherichia coli with AK-TAG. PLoS One, 2016, 11(5): e0156106.
doi: 10.1371/journal.pone.0156106
|
[40] |
Mamat U, Wilke K, Bramhill D, et al. Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins. Microbial Cell Factories, 2015, 14: 57.
doi: 10.1186/s12934-015-0241-5
pmid: 25890161
|
[41] |
Ulrichts H, Silence K, Schoolmeester A, et al. Antithrombotic drug candidate ALX-0081 shows superior preclinical efficacy and safety compared with currently marketed antiplatelet drugs. Blood, 2011, 118(3): 757-765.
doi: 10.1182/blood-2010-11-317859
pmid: 21576702
|
[42] |
Wan R R, Liu A Q, Hou X Q, et al. Screening and antitumor effect of an anti-CTLA-4 nanobody. Oncology Reports, 2018, 39(2): 511-518.
|
[43] |
Papadopoulos K P, Isaacs R, Bilic S, et al. Unexpected hepatotoxicity in a phase I study of TAS266, a novel tetravalent agonistic Nanobody® targeting the DR5 receptor. Cancer Chemotherapy and Pharmacology, 2015, 75(5): 887-895.
doi: 10.1007/s00280-015-2712-0
pmid: 25721064
|
[44] |
de Bruin R C G, Veluchamy J P, Lougheed S M, et al. A bispecific nanobody approach to leverage the potent and widely applicable tumor cytolytic capacity of Vγ9Vδ2-T cells. Oncoimmunology, 2017, 7(1): e1375641.
doi: 10.1080/2162402X.2017.1375641
|
[45] |
Xenaki K T, Dorrestijn B, Muns J A, et al. Homogeneous tumor targeting with a single dose of HER2-targeted albumin-binding domain-fused nanobody-drug conjugates results in long-lasting tumor remission in mice. Theranostics, 2021, 11(11): 5525-5538.
doi: 10.7150/thno.57510
pmid: 33859761
|
[46] |
Lennart Z, Annick V, Dominiek C, et al. Selection of non-competitive leptin antagonists using a random nanobody-based approach. The Biochemical Journal, 2012, 441(1): 425-34.
doi: 10.1042/BJ20110438
|
[47] |
Kaczmarek J Z, Skottrup P D. Selection and characterization of camelid nanobodies towards urokinase-type plasminogen activator. Molecular Immunology, 2015, 65(2): 384-390.
doi: 10.1016/j.molimm.2015.02.011
pmid: 25749705
|
[48] |
Fan J S, Zhuang X L, Yang X Y, et al. A multivalent biparatopic EGFR-targeting nanobody drug conjugate displays potent anticancer activity in solid tumor models. Signal Transduction and Targeted Therapy, 2021, 6: 320.
doi: 10.1038/s41392-021-00666-5
pmid: 34475375
|
[49] |
Nikkhoi S K, Rahbarizadeh F, Ranjbar S, et al. Liposomal nanoparticle armed with bivalent bispecific single-domain antibodies, novel weapon in HER2 positive cancerous cell lines targeting. Molecular Immunology, 2018, 96: 98-109.
doi: S0161-5890(18)30017-8
pmid: 29549861
|
[50] |
Ding L, Tian C P, Feng S, et al. Small sized EGFR1 and HER2 specific bifunctional antibody for targeted cancer therapy. Theranostics, 2015, 5(4): 378-398.
doi: 10.7150/thno.10084
pmid: 25699098
|
[51] |
Yang Z Y, Schmidt D, Liu W L, et al. A novel multivalent, single-domain antibody targeting TcdA and TcdB prevents fulminant Clostridium difficile infection in mice. The Journal of Infectious Diseases, 2014, 210(6): 964-972.
doi: 10.1093/infdis/jiu196
|
[52] |
Steeland S, Puimège L, Vandenbroucke R E, et al. Generation and characterization of small single domain antibodies inhibiting human tumor necrosis factor receptor 1. The Journal of Biological Chemistry, 2015, 290(7): 4022-4037.
doi: 10.1074/jbc.M114.617787
|
[53] |
Hmila I, Saerens D, Ben Abderrazek R, et al. A bispecific nanobody to provide full protection against lethal scorpion envenoming. The FASEB Journal, 2010, 24(9): 3479-3489.
doi: 10.1096/fsb2.v24.9
|
[54] |
Cristina H, Tremblay Jacqueline M, Shoemaker Charles B, et al. Mechanisms of ricin toxin neutralization revealed through engineered homodimeric and heterodimeric camelid antibodies. The Journal of Biological Chemistry, 2015, 290(46): 27880-27889.
doi: 10.1074/jbc.M115.658070
|
[55] |
Yin J C, Li G X, Ren X F, et al. Select what You need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. Journal of Biotechnology, 2007, 127(3): 335-347.
pmid: 16959350
|
[56] |
Mattanovich D, Branduardi P, Dato L, et al. Recombinant protein production in yeasts. Methods in Molecular Biology, 2012, 824: 329-358.
doi: 10.1007/978-1-61779-433-9_17
pmid: 22160907
|
[57] |
Tyo K E J, Liu Z H, Magnusson Y, et al. Impact of protein uptake and degradation on recombinant protein secretion in yeast. Applied Microbiology and Biotechnology, 2014, 98(16): 7149-7159.
doi: 10.1007/s00253-014-5783-7
pmid: 24816620
|
[58] |
Cereghino G P L, Cregg J M. Applications of yeast in biotechnology: protein production and genetic analysis. Current Opinion in Biotechnology, 1999, 10(5): 422-427.
pmid: 10508632
|
[59] |
Rachel D, Hearn Milton T W. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. Journal of Molecular Recognition: JMR, 2005, 18(2): 119-138.
doi: 10.1002/(ISSN)1099-1352
|
[60] |
Gerngross T U. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nature Biotechnology, 2004, 22(11): 1409-1414.
pmid: 15529166
|
[61] |
Roghayyeh B, Mousavi G S L, Masoumeh R, et al. Camelid-derived heavy-chain nanobody against Clostridium botulinum neurotoxin E in Pichia pastoris. Biotechnology and Applied Biochemistry, 2016, 63(2): 200-205.
doi: 10.1002/bab.1226
pmid: 24673401
|
[62] |
Shahrbanoo P, Latif M G S, Masoumeh R, et al. Efficient production of nanobodies against urease activity of Helicobacter pylori in Pichia pastoris. Turkish Journal of Medical Sciences, 2017, 47(2): 695-701.
doi: 10.3906/sag-1509-121
pmid: 28425268
|
[63] |
Emberson L M, Trivett A J, Blower P J, et al. Expression of an anti-CD 33 single-chain antibody by Pichia pastoris. Journal of Immunological Methods, 2005, 305(2): 135-151.
pmid: 16139294
|
[64] |
Baghban R, Farajnia S, Ghasemi Y, et al. New developments in Pichia pastoris expression system, review and update. Current Pharmaceutical Biotechnology, 2018, 19(6): 451-467.
doi: 10.2174/1389201019666180718093037
|
[65] |
van Roy M, Ververken C, Beirnaert E, et al. The preclinical pharmacology of the high affinity anti-IL-6R Nanobody® ALX-0061 supports its clinical development in rheumatoid arthritis. Arthritis Research & Therapy, 2015, 17(1): 135.
|
[66] |
Holz J B, Sargentini L, Bruyn S, et al. OP0043 twenty-four weeks of treatment with a novel anti-IL-6 receptor nanobody® (ALX-0061) resulted in 84% ACR20 improvement and 58% DAS28 remission in a phase i/ii study in RA. Annals of the Rheumatic Diseases, 2014, 72: A64-A64.
doi: 10.1136/annrheumdis-2013-eular.23
|
[67] |
Detalle L, Stohr T, Palomo C, et al. Generation and characterization of ALX-0171, a potent novel therapeutic nanobody for the treatment of respiratory syncytial virus infection. Antimicrobial Agents and Chemotherapy, 2016, 60(1): 6-13.
doi: 10.1128/AAC.01802-15
pmid: 26438495
|
[68] |
Ahmad Parray H, Shukla S, Perween R, et al. Inhalation monoclonal antibody therapy: a new way to treat and manage respiratory infections. Applied Microbiology and Biotechnology, 2021, 105(16): 6315-6332.
doi: 10.1007/s00253-021-11488-4
|
[69] |
Liu S, Li G H, Ding L, et al. Evaluation of SARS-CoV-2-neutralizing nanobody using virus receptor binding domain-administered model mice. Research, 2022, 2022: 9864089.
|
[70] |
Wan Y, Gai J, Zhu M, et al. Phase I safety and efficacy evaluation of the first-in-class inhalable anti-IL-4Rα single domain antibody, A33//Late Breaking Advances in Asthma and Immunology. San Francisco :American Thoracic Society, 2023: A1379-A1379.
|
[71] |
Mochizuki S, Hamato N, Hirose M, et al. Expression and characterization of recombinant human antithrombin III in Pichia pastoris. Protein Expression and Purification, 2001, 23(1): 55-65.
pmid: 11570846
|
[72] |
Gemmill T R, Trimble R B. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochimica et Biophysica Acta (BBA) - General Subjects, 1999, 1426(2): 227-237.
doi: 10.1016/S0304-4165(98)00126-3
|
[73] |
Dean N. Asparagine-linked glycosylation in the yeast Golgi. Biochimica et Biophysica Acta (BBA) - General Subjects, 1999, 1426(2): 309-322.
doi: 10.1016/S0304-4165(98)00132-9
|
[74] |
Wildt S, Gerngross T U. The humanization of N-glycosylation pathways in yeast. Nature Reviews Microbiology, 2005, 3(2): 119-128.
doi: 10.1038/nrmicro1087
|
[75] |
Parsaie Nasab F, Aebi M, Bernhard G, et al. A combined system for engineering glycosylation efficiency and glycan structure in Saccharomyces cerevisiae. Applied and Environmental Microbiology, 2013, 79(3): 997-1007.
doi: 10.1128/AEM.02817-12
|
[76] |
Gai J W, Ma L L, Li G H, et al. A potent neutralizing nanobody against SARS-CoV-2 with inhaled delivery potential. MedComm, 2021, 2(1): 101-113.
doi: 10.1002/mco2.60
pmid: 33821254
|
[77] |
Roberts K J, Cubitt M F, Carlton T M, et al. Preclinical development of a bispecific TNFα/IL-23 neutralising domain antibody as a novel oral treatment for inflammatory bowel disease. Scientific Reports, 2021, 11: 19422.
doi: 10.1038/s41598-021-97236-0
pmid: 34593832
|
[78] |
Terryn S, Francart A, Lamoral S, et al. Protective effect of different anti-rabies virus VHH constructs against rabies disease in mice. PLoS One, 2014, 9(10): e109367.
doi: 10.1371/journal.pone.0109367
|
[79] |
Günaydın G, Yu S Z, Gräslund T, et al. Fusion of the mouse IgG 1 Fc domain to the VHH fragment (ARP1) enhances protection in a mouse model of rotavirus. Scientific Reports, 2016, 6: 30171.
doi: 10.1038/srep30171
pmid: 27439689
|
[80] |
Pant N, Marcotte H, Hermans P, et al. Lactobacilli producing bispecific llama-derived anti-rotavirus proteins in vivo for rotavirus-induced diarrhea. Future Microbiology, 2011, 6(5): 583-593.
doi: 10.2217/fmb.11.32
|
[81] |
Ji X M, Lu W G, Zhou H T, et al. Covalently dimerized Camelidae antihuman TNFa single-domain antibodies expressed in yeast Pichia pastoris show superior neutralizing activity. Applied Microbiology and Biotechnology, 2013, 97(19): 8547-8558.
doi: 10.1007/s00253-012-4639-2
|
[82] |
Ezzine A, M’Hirsi el Adab S, Bouhaouala-Zahar B, et al. Efficient expression of the anti-AahI’ scorpion toxin nanobody under a new functional form in a Pichia pastoris system. Biotechnology and Applied Biochemistry, 2012, 59(1): 15-21.
doi: 10.1002/bab.67
pmid: 22332740
|
[83] |
Pan H C, Su Y N, Xie Y N, et al. Everestmab, a novel long-acting GLP-1/anti GLP-1R nanobody fusion protein, exerts potent anti-diabetic effects. Artificial Cells, Nanomedicine, and Biotechnology, 2020, 48(1): 854-866.
doi: 10.1080/21691401.2020.1770268
|
[84] |
Hofmeyer T, Bulani S I, Grzeschik J, et al. Protein production in Yarrowia lipolytica via fusion to the secreted lipase Lip2p. Molecular Biotechnology, 2014, 56(1): 79-90.
doi: 10.1007/s12033-013-9684-2
pmid: 23852986
|
[85] |
Adams H, Horrevoets W M, Adema S M, et al. Inhibition of biofilm formation by Camelid single-domain antibodies against the flagellum of Pseudomonas aeruginosa. Journal of Biotechnology, 2014, 186: 66-73.
doi: 10.1016/j.jbiotec.2014.06.029
|
[86] |
Stolfa G, Smonskey M T, Boniface R, et al. CHO-omics review: the impact of current and emerging technologies on Chinese hamster ovary based bioproduction. Biotechnology Journal, 2018, 13(3): e1700227.
|
[87] |
Swiech K, Picanço-Castro V, Covas D T. Human cells: new platform for recombinant therapeutic protein production. Protein Expression and Purification, 2012, 84(1): 147-153.
doi: 10.1016/j.pep.2012.04.023
pmid: 22580292
|
[88] |
Ghaderi D, Zhang M, Hurtado-Ziola N, et al. Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation. Biotechnology & Genetic Engineering Reviews, 2012, 28: 147-175.
|
[89] |
Durocher Y, Butler M. Expression systems for therapeutic glycoprotein production. Current Opinion in Biotechnology, 2009, 20(6): 700-707.
doi: 10.1016/j.copbio.2009.10.008
pmid: 19889531
|
[90] |
Markham A. Envafolimab: first approval. Drugs, 2022, 82(2): 235-240.
doi: 10.1007/s40265-022-01671-w
pmid: 35122636
|
[91] |
Manier S, Ingegnere T, Escure G, et al. Current state and next-generation CAR-T cells in multiple myeloma. Blood Reviews, 2022, 54: 100929.
doi: 10.1016/j.blre.2022.100929
|
[92] |
Salvador J P, Vilaplana L, Marco M P. Nanobody: outstanding features for diagnostic and therapeutic applications. Analytical and Bioanalytical Chemistry, 2019, 411(9): 1703-1713.
doi: 10.1007/s00216-019-01633-4
pmid: 30734854
|
[93] |
Bobkov V, Zarca A M, Van Hout A, et al. Nanobody-Fc constructs targeting chemokine receptor CXCR4 potently inhibit signaling and CXCR4-mediated HIV-entry and induce antibody effector functions. Biochemical Pharmacology, 2018, 158: 413-424.
doi: S0006-2952(18)30435-0
pmid: 30342023
|
[94] |
Wu X L, Li Y L, Huang B L, et al. A single-domain antibody inhibits SFTSV and mitigates virus-induced pathogenesis in vivo. JCI Insight, 2020, 5(13): e136855.
doi: 10.1172/jci.insight.136855
|
[95] |
Xun G J, Song X P, Hu J E, et al. Potent human single-domain antibodies specific for a novel prefusion epitope of respiratory syncytial virus F glycoprotein. Journal of Virology, 2021, 95(18): e0048521.
doi: 10.1128/JVI.00485-21
|
[96] |
Lu Q Z, Zhang Z L, Li H X, et al. Development of multivalent nanobodies blocking SARS-CoV-2 infection by targeting RBD of spike protein. Journal of Nanobiotechnology, 2021, 19(1): 33.
doi: 10.1186/s12951-021-00768-w
pmid: 33514385
|
[97] |
Vandesquille M, Li T F, Po C, et al. Chemically-defined camelid antibody bioconjugate for the magnetic resonance imaging of Alzheimer’s disease. mAbs, 2017, 9(6): 1016-1027.
doi: 10.1080/19420862.2017.1342914
pmid: 28657418
|
[98] |
Bao C, Gao Q L, Li L L, et al. The application of nanobody in CAR-T therapy. Biomolecules, 2021, 11(2): 238.
doi: 10.3390/biom11020238
|
[99] |
Jiang H P, Ni H Q, Zhang P, et al. PD-L1/LAG-3 bispecific antibody enhances tumor-specific immunity. Oncoimmunology, 2021, 10(1): 1943180.
doi: 10.1080/2162402X.2021.1943180
|
[100] |
Wang Y, Ni H Q, Zhou S X, et al. Tumor-selective blockade of CD 47 signaling with a CD47/PD-L1 bispecific antibody for enhanced anti-tumor activity and limited toxicity. Cancer Immunology, Immunotherapy, 2021, 70(2): 365-376.
doi: 10.1007/s00262-020-02679-5
|
[101] |
Abe M, Yuki Y, Kurokawa S, et al. A rice-based soluble form of a murine TNF-specific llama variable domain of heavy-chain antibody suppresses collagen-induced arthritis in mice. Journal of Biotechnology, 2014, 175: 45-52.
doi: 10.1016/j.jbiotec.2014.02.005
pmid: 24548461
|
[102] |
Pant N, Hultberg A, Zhao Y F, et al. Lactobacilli expressing variable domain of llama heavy-chain antibody fragments (lactobodies) confer protection against rotavirus-induced diarrhea. The Journal of Infectious Diseases, 2006, 194(11): 1580-1588.
doi: 10.1086/jid.2006.194.issue-11
|
[103] |
Mizukami M, Tokunaga H, Onishi H, et al. Highly efficient production of VHH antibody fragments in Brevibacillus choshinensis expression system. Protein Expression and Purification, 2015, 105: 23-32.
doi: 10.1016/j.pep.2014.09.017
pmid: 25286401
|
[104] |
Okazaki F, Aoki J I, Tabuchi S, et al. Efficient heterologous expression and secretion in Aspergillus oryzae of a llama variable heavy-chain antibody fragment VHH against EGFR. Applied Microbiology and Biotechnology, 2012, 96(1): 81-88.
doi: 10.1007/s00253-012-4158-1
|
[105] |
Hisada H, Tsutsumi H, Ishida H, et al. High production of llama variable heavy-chain antibody fragment (VHH) fused to various reader proteins by Aspergillus oryzae. Applied Microbiology and Biotechnology, 2013, 97(2): 761-766.
doi: 10.1007/s00253-012-4211-0
|
[106] |
Gomord V, Fitchette A C, Menu-Bouaouiche L, et al. Plant-specific glycosylation patterns in the context of therapeutic protein production. Plant Biotechnology Journal, 2010, 8(5): 564-587.
doi: 10.1111/j.1467-7652.2009.00497.x
pmid: 20233335
|
[107] |
Tschofen M, Knopp D, Hood E, et al. Plant molecular farming: much more than medicines. Annual Review of Analytical Chemistry (Palo Alto, Calif), 2016, 9(1): 271-294.
doi: 10.1146/anchem.2016.9.issue-1
|
[108] |
Łojewska E, Kowalczyk T, Olejniczak S, et al. Extraction and purification methods in downstream processing of plant-based recombinant proteins. Protein Expression and Purification, 2016, 120: 110-117.
doi: 10.1016/j.pep.2015.12.018
pmid: 26742898
|
[109] |
Lim C Y, Lee K J, Oh D B, et al. Effect of the developmental stage and tissue position on the expression and glycosylation of recombinant glycoprotein GA733-FcK in transgenic plants. Frontiers in Plant Science, 2014, 5: 778.
|
[110] |
Park S R, Lee J H, Kim K, et al. Expression and in vitro function of anti-breast cancer llama-based single domain antibody VHH expressed in tobacco plants. International Journal of Molecular Sciences, 2020, 21(4): 1354.
doi: 10.3390/ijms21041354
|
[111] |
Whaley K J, Hiatt A, Zeitlin L. Emerging antibody products and Nicotiana manufacturing. Human Vaccines, 2011, 7(3): 349-356.
doi: 10.4161/hv.7.3.14266
pmid: 21358287
|
[112] |
Conrad U, Plagmann I, Malchow S, et al. ELPylated anti-human TNF therapeutic single-domain antibodies for prevention of lethal septic shock. Plant Biotechnology Journal, 2011, 9(1): 22-31.
doi: 10.1111/j.1467-7652.2010.00523.x
pmid: 20444206
|
[113] |
Teh Y H A, Kavanagh T A. High-level expression of Camelid nanobodies in Nicotiana benthamiana. Transgenic Research, 2010, 19(4): 575-586.
doi: 10.1007/s11248-009-9338-0
|
[114] |
Barrera D J, Rosenberg J N, Chiu J G, et al. Algal chloroplast produced camelid VHH antitoxins are capable of neutralizing botulinum neurotoxin. Plant Biotechnology Journal, 2015, 13(1): 117-124.
doi: 10.1111/pbi.12244
pmid: 25229405
|
[115] |
Modarresi M, Javaran M J, Shams-bakhsh M, et al. Transient expression of anti-VEFGR2 nanobody in Nicotiana tabacum and N. benthamiana. 3 Biotech, 2018, 8(12): 484.
doi: 10.1007/s13205-018-1500-z
pmid: 30467531
|
[116] |
Morello E, Bermúdez-Humarán L G, Llull D, et al. Lactococcus lactis, an efficient cell factory for recombinant protein production and secretion. Journal of Molecular Microbiology and Biotechnology, 2008, 14(1-3): 48-58.
pmid: 17957110
|
[117] |
Andersen K K, Strokappe N M, Hultberg A, et al. Neutralization of Clostridium difficile toxin B mediated by engineered lactobacilli that produce single-domain antibodies. Infection and Immunity, 2016, 84(2): 395-406.
doi: 10.1128/IAI.00870-15
pmid: 26573738
|
[118] |
Cérutti M, Golay J. Lepidopteran cells, an alternative for the production of recombinant antibodies? mAbs, 2012, 4(3): 294-309.
doi: 10.4161/mabs.19942
pmid: 22531440
|
[119] |
Gecchele E, Merlin M, Brozzetti A, et al. A comparative analysis of recombinant protein expression in different biofactories: bacteria, insect cells and plant systems. Journal of Visualized Experiments, 2015(97): e52459.
|
[120] |
Contreras-Gómez A, Sánchez-Mirón A, García-Camacho F, et al. Protein production using the baculovirus-insect cell expression system. Biotechnology Progress, 2014, 30(1): 1-18.
pmid: 24265112
|
[121] |
Le L T M, Nyengaard J R, Golas M M, et al. Vectors for expression of signal peptide-dependent proteins in baculovirus/insect cell systems and their application to expression and purification of the high-affinity immunoglobulin gamma Fc receptor I in complex with its gamma chain. Molecular Biotechnology, 2018, 60(1): 31-40.
doi: 10.1007/s12033-017-0041-8
pmid: 29143175
|
[122] |
Gómez-Sebastián S, Nuñez M C, Garaicoechea L, et al. Rotavirus A-specific single-domain antibodies produced in baculovirus-infected insect larvae are protective in vivo. BMC Biotechnology, 2012, 12: 59.
pmid: 22953695
|
[123] |
Narjes S, Mahdi H, Ali J, et al. Expressing of recombinant VEGFR2-specific nanobody in baculovirus expression system. Iranian Journal of Biotechnology, 2021, 19(1): e2783.
doi: 10.30498/IJB.2021.2783
pmid: 34179196
|
[124] |
Magaña-Ortíz D, Fernández F, Loske A M, et al. Extracellular expression in Aspergillus niger of an antibody fused to Leishmania sp. antigens. Current Microbiology, 2018, 75(1): 40-48.
doi: 10.1007/s00284-017-1348-1
pmid: 28861662
|
[125] |
Havlik D, Brandt U, Bohle K, et al. Establishment of Neurospora crassa as a host for heterologous protein production using a human antibody fragment as a model product. Microbial Cell Factories, 2017, 16(1): 1-15.
doi: 10.1186/s12934-016-0616-2
|
[126] |
Anyaogu D C, Mortensen U H. Manipulating the glycosylation pathway in bacterial and lower eukaryotes for production of therapeutic proteins. Current Opinion in Biotechnology, 2015, 36: 122-128.
doi: 10.1016/j.copbio.2015.08.012
pmid: 26340101
|
[127] |
Zubieta M P, Contesini F J, Rubio M V, et al. Protein profile in Aspergillus nidulans recombinant strains overproducing heterologous enzymes. Microbial Biotechnology, 2018, 11(2): 346-358.
doi: 10.1111/mbt2.2018.11.issue-2
|
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
|
Shared |
|
|
|
|
|
Discussed |
|
|
|
|