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Production platforms for biotherapeutic glycoproteins. Occurrence impact, and challenges of non-human sialylation
Open accessAbstract
One of the fastest growing fields in the pharmaceutical industry is the market for therapeutic glycoproteins. Today, these molecules play a major role in the treatment of various diseases, and include several protein classes, i.e., clotting factors, hormones, cytokines, antisera, enzymes, enzyme inhibitors, Ig-Fc-Fusion proteins, and monoclonal antibodies. Optimal glycosylation is critical for therapeutic glycoproteins, as glycans can influence their yield, immunogenicity and efficacy, which impact the costs and success of such treatments. While several mammalian cell expression systems currently used can produce therapeutic glycoproteins that are mostly decorated with human-like glycans, they can differ from human glycans by presenting two structures at the terminal and therefore most exposed position. First, natural human N-glycans are lacking the terminal Gal 1-3Gal (alpha-Gal) modification; and second, they do not contain the non-human sialic acid N-glycolylneuraminic acid (Neu5Gc). All humans spontaneously express antibodies against both of these glycan structures, risking increased immunogenicity of biotherapeutics carrying such non-human glycan epitopes. However, in striking contrast to the alpha-Gal epitope, exogenous Neu5Gc can be metabolically incorporated into human cells and presented on expressed glycoproteins in several possible epitopes. Recent work has demonstrated that this non-human sialic acid is found in widely varying amounts on biotherapeutic glycoproteins approved for treatment of various medical conditions. Neu5Gc on glycans of these medical agents likely originates from the production process involving the non-human mammalian cell lines and/or the addition of animal-derived tissue culture supplements. Further studies are needed to fully understand the impact of Neu5Gc in biotherapeutic agents. Similar concerns apply to human cells prepared for allo- or auto-transplantation, that have been grown in animal-derived tissue culture supplements.
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“Indeed, plants produce core α1,3-fructose and β1,2-xylose, which are completely absent in human cells and could be immunogenic (Karg et al., 2009;Ghaderi et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Ghaderi et al., 2012
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Cites
Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,089
Siglecs and their roles in the immune system
Crocker, P. R., Paulson, J. C., & Varki, A. P. (2007) · Nature reviews. Immunology · doi:10.1038/nri2056 · Cited by 2,032
Self-citationCetuximab-Induced Anaphylaxis and IgE Specific for Galactose-α-1,3-Galactose
Chung, C. H., Mirakhur, B., Chan, E., Le, Q.-T., Berlin, J., Morse, M., Murphy, B. A., Satinover, S. M., Hosen, J., Mauro, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa074943 · Cited by 1,521
The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins
Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., & Dwek, R. A. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141702 · Cited by 1,354
Chemical Diversity in the Sialic Acids and Related α-Keto Acids: An Evolutionary Perspective
Angata, T., & Varki, A. P. (2002) · Chemical Reviews · doi:10.1021/cr000407m · Cited by 1,254
Self-citationProduction of α1,3-Galactosyltransferase-Deficient Pigs
Phelps, C. J., Koike, C., Vaught, T. D., Boone, J. T., Wells, K. D., Chen, S.-H., Ball, S. F., Specht, S. M., Polejaeva, I. A., Monahan, J. A., et al. (2003) · Science · doi:10.1126/science.1078942 · Cited by 1,111
Baculovirus as versatile vectors for protein expression in insect and mammalian cells
Kost, T. A., Condreay, J. P., & Jarvis, D. L. (2005) · Nature Biotechnology · doi:10.1038/nbt1095 · Cited by 1,014
Human embryonic stem cells express an immunogenic nonhuman sialic acid
Martin, M. J., Muotri, A. R., Gage, F. H., & Varki, A. P. (2005) · Nature Medicine · doi:10.1038/nm1181 · Cited by 935
Self-citationJournal of the National Cancer Institute
(1993) · Journal of the American Dietetic Association · doi:10.1016/0002-8223(93)92324-q · Cited by 913
Wiseman, M. J. (2008) · Proceedings of The Nutrition Society · doi:10.1017/s002966510800712x · Cited by 902
Flagged first, then by citations
Research works printed but not linked: 7
- Borys MC, 2009, Biotechnol Bioeng
- Dahl SL, 2011, Sci Transl Med, 3
- Hanganutziu M, 1924, CR Séances Soc Biol, 91, 1457
- Higashi H, 1985, Cancer Research, 45, 3796
- Stanley P, 2009, Essentials of Glycobiology, 101
- Takiguchi M, 1984, Clin Exp Immunol, 56, 345
- Varki A, 2009, Essentials of Glycobiology, 281
Cited by
Sorted by citations
Items 201–300 of 321
Miyajima, R., Manaka, H., Honda, T., Hashii, N., Suzuki, M., Komeno, M., Takao, K., Ishii‐Watabe, A., Igarashi, K., Toida, T., et al. (2023) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2023.10.008 · Cited by 6
Egashira, Y., Nagatoishi, S., Kiyoshi, M., Ishii‐Watabe, A., & Tsumoto, K. (2018) · The Journal of Biochemistry · doi:10.1093/jb/mvy021 · Cited by 6
Bacterial Artificial Chromosome-based Protein Expression Platform Using the Tol2 Transposon System
Kuk, M. U., Park, J. Y., Song, E. S., Lee, Y. H., Lee, Y. H., Joo, J., Kwon, H. W., & Park, J. T. (2022) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-021-0222-y · Cited by 6
Design of Glycoengineered IL-4 Antagonists Employing Chemical and Biosynthetic Glycosylation
Thomas, S., Fiebig, J. E., Kuhn, E.-M., Mayer, D. S., Filbeck, S., Schmitz, W., Krischke, M., Gropp, R., & Mueller, T. D. (2023) · ACS Omega · doi:10.1021/acsomega.3c00726 · Cited by 6
Glycoprofile Comparison of the SARS-CoV-2 Spike Proteins Expressed in CHO and HEK Cell Lines
Wright, H. L., Evans, C. A., Jackson, P. J., James, D. C., Tee, K. L., Wong, T. S., Dickman, M. J., & Pandhal, J. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01288-2 · Cited by 6
Chen, X., Liu, J., Liu, X., Li, F., Zhao, L., & Tan, W. (2018) · Process Biochemistry · doi:10.1016/j.procbio.2018.08.015 · Cited by 6
More comprehensive standards for monitoring glycosylation.
Guo, J.-Z., Tu, H., Rao, B. M., Chillara, A. K., Chang, E., & Atouf, F. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113896 · Cited by 6
Pivotal Biology, Chemistry, Biochemistry, and Biophysical Concepts of Biologics and Biosimilars
Kayser, V., & Reslan, M. (2020) · Wiley eBooks · doi:10.1002/9781119564690.ch6 · Cited by 6
Panda, S., Swain, S. K., Sahu, B. P., Mahapatra, S. R., Dey, J., Sarangi, R., Ranade, A. V., & Mishra, N. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1513245 · Cited by 5
Grassi, L., Harris, C. L., Zhu, J., Hardman, C. H., & Hatton, D. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab366 · Cited by 5
Shin, S. W., Kyeong, M., & Lee, J. S. (2021) · Cell engineering · doi:10.1007/978-3-030-79871-0_7 · Cited by 5
Wang, S., Tian, H., Tian, P., Xing, Y., & Zeng, Y. (2024) · Translational Cancer Research · doi:10.21037/tcr-23-1371 · Cited by 6
Applying Acylated Fucose Analogues to Metabolic Glycoengineering
Rosenlöcher, J., Böhrsch, V., Sacharjat, M., Blanchard, V., Giese, C., Sandig, V., Hackenberger, C. P. R., & Hinderlich, S. (2015) · Bioengineering · doi:10.3390/bioengineering2040213 · Cited by 5
Protein Production in Eukaryotic Cells
Ram, K., Hatton, D., Ahuja, S., Bender, J., Hunter, A. K., & Turner, R. C. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2016_3 · Cited by 5
Xu, S., Borys, M., Khetan, A., & Pla, I. (2020) · Biotechnology Progress · doi:10.1002/btpr.3038 · Cited by 5
Cha, H.-M., Hwang, J.-M., Yeon, J.-H., Lim, J.-H., Han, H., & Kim, D. (2021) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-020-0389-7 · Cited by 5
Biosimilars Drug Substance Development and Manufacturing: Effective CMC Strategy
Manzi, A. E., & Ultee, M. E. (2018) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-319-99680-6_8 · Cited by 5
Expression and Characterisation of Recombinant Molecules in Transgenic Soybean
da Cunha, N. B., Murad, A. M., Vianna, G. R., Coelho, C. M., & Rech, E. L. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319310010 · Cited by 5
MS‐Based Glycome Characterization of Biotherapeutics With N‐ and O‐Glycosylation
Oh, M. J., Seo, Y., Seo, N., & An, H. J. (2025) · Mass Spectrometry Reviews · doi:10.1002/mas.21925 · Cited by 5
Wei, W., Kim, J. M., Medina, D., Lakatta, E. G., & Li, L. (2013) · Protein Expression and Purification · doi:10.1016/j.pep.2013.12.006 · Cited by 4
Misaki, R., Iwasaki, M., Takechi, H., Yamano, N., Ohashi, T., Kajiura, H., & Fujiyama, K. (2022) · Cytotechnology · doi:10.1007/s10616-021-00501-3 · Cited by 4
A versatile design platform for glycoengineering therapeutic antibodies
Ludwig, S. D., Bernstein, Z. J., Agatemor, C., Dammen‐Brower, K., Ruffolo, J. A., Rosas, J. M., Post, J. D., Cole, R. N., Yarema, K. J., & Spangler, J. B. (2022) · mAbs · doi:10.1080/19420862.2022.2095704 · Cited by 4
Using endoplasmic reticulum engineering to improve recombinant protein production in CHO cells
Zhang, J., Wang, W., Zhang, X., Wang, F., Geng, S., Wang, X., & Wang, T. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144695 · Cited by 4
Vukušić, K. (2016) · Periodicum Biologorum · doi:10.18054/pb.2016.118.2.3845 · Cited by 4
Monoclonal Antibodies: Mechanisms of Action
Jefferis, R. (2014) · ACS symposium series · doi:10.1021/bk-2014-1176.ch002 · Cited by 5
Enhanced expression of a biosimilar monoclonal antibody with a novel NS0 platform
Sampey, D. B., Courville, P., Acree, D., Hausfeld, J. N., & Bentley, W. E. (2018) · Biotechnology Progress · doi:10.1002/btpr.2596 · Cited by 4
Enatsu, H., Okamoto, N., Nomura, Y., Onitsuka, M., Yamano, N., Koga, Y., & Ōmasa, T. (2021) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2021.04.015 · Cited by 4
Rapid Antibody Glycoengineering in CHO Cells Via RNA Interference and CGE-LIF N-Glycomics
Kotidis, P., Marbiah, M. M., Donini, R., Gómez, I. A., del Val, I. J., Haslam, S. M., Polizzi, K. M., & Kontoravdi, C. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1685-7_7 · Cited by 3
Duran, A., Guerrero, P. E., Ortiz, M., del Campo, D. P., Castro, E., Garcia-Velasco, A., Fort, E., Llorens, R., Saldova, R., Llop, E., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10081942 · Cited by 4
Afonja, O., Kozak, R. W., Petraro, P., Michaels, L. A., Mathew, P., Lemm, G., & Kessler, C. M. (2016) · Expert Review of Hematology · doi:10.1080/17474086.2017.1259559 · Cited by 4
Biologics: structural heterogeneity and immunogenicity
Jefferis, R. (2017) · British Journal of Hospital Medicine · doi:10.12968/hmed.2017.78.8.443 · Cited by 4
An automated data‐driven DSP development approach for glycoproteins from yeast
Rajamanickam, V., Krippl, M., Herwig, C., & Oliver Spadiut, A. (2017) · Electrophoresis · doi:10.1002/elps.201700229 · Cited by 4
Biopharmaceuticals Produced from Cultivated Mammalian Cells
Al‐Majmaie, R., Kuystermans, D., & Al‐Rubeai, M. (2021) · Cell engineering · doi:10.1007/978-3-030-79871-0_1 · Cited by 4
Rosenlöcher, J., Weilandt, C., Sandig, G., Reinke, S. O., Blanchard, V., & Hinderlich, S. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.08.008 · Cited by 4
Genetic Divergence and Antibody Expression Influence the N‐Glycomes of CHO‐K1 and CHO‐S Cells
Donini, R., Blundell, P. A., Pleass, R. J., Lu, D., Dell, A., Kontoravdi, C., & Haslam, S. M. (2025) · Biotechnology and Bioengineering · doi:10.1002/bit.70045 · Cited by 3
Zeerleder, S. S., Engel, R., Zhang, T., Roem, D., van Mierlo, G. J., Bos, I. G. A. C., van Ham, S. M., Wuhrer, M., Wouters, D., & Jongerius, I. (2021) · Pharmaceuticals · doi:10.3390/ph14010054 · Cited by 3
Sran, K. S., Sharma, Y., Kaur, T., & Rao, A. (2022) · Journal of Proteins and Proteomics · doi:10.1007/s42485-022-00086-1 · Cited by 3
One‐step production of fully biotinylated and glycosylated human Fc gamma receptors
Kang, M., Wang, Z., & Ge, X. (2023) · Biotechnology Progress · doi:10.1002/btpr.3392 · Cited by 3
Makey, D. M., & Ruotolo, B. T. (2024) · Expert Review of Proteomics · doi:10.1080/14789450.2024.2373707 · Cited by 3
Development of Magoh protein‐overexpressing HEK cells for optimized therapeutic protein production
Mufarrege, E. F., Benizio, E., Prieto, C. C., Chiappini, F. A., Rodríguez, M. C., Etcheverrigaray, M., & Kratje, R. B. (2020) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1915 · Cited by 3
Stable, high yield expression of gp145 Env glycoprotein from HIV-1 in mammalian cells
Luthra, A., Cheema, S., Whitney, S., Bakker, W. A. M., Sandalon, Z., Richardson, J. C., Yallop, C., & Havenga, M. J. E. (2021) · Biologicals · doi:10.1016/j.biologicals.2021.07.004 · Cited by 3
Bahadori, M., Amiri, F., Movahed, M., Roushandeh, A. M., & Roudkenar, M. H. (2017) · Gene Cell and Tissue · doi:10.5812/gct.13360 · Cited by 3
Isolation of recombinant human antithrombin isoforms by Cellufine Sulfate affinity chromatography
Sugihara, T., Fujiwara, S., Ishioka, S., Urakubo, T., & Suzawa, T. (2018) · Journal of Chromatography B · doi:10.1016/j.jchromb.2018.07.001 · Cited by 3
Tabasinezhad, M., Mahboudi, F., Wenzel, W., Rahimi, H., Walther, T. H., Blattner, C., & Omidinia, E. (2018) · Protein Expression and Purification · doi:10.1016/j.pep.2018.11.006 · Cited by 3
Silva, L. C., dos Santos, M. H., Heluy, T. R., Biaggio, R. T., Ferreira, A. R., Milhomens, J., Kashima, S. H., Nemer, W. E., Hoss, S. E., Picanço‐Castro, V., et al. (2020) · Engineering Reports · doi:10.1002/eng2.12172 · Cited by 3
Reķēna, A., Livkisa, D., Kamolins, E., Vanags, J., & Loča, D. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.751538 · Cited by 3
Resolving domain positions of cellobiose dehydrogenase by small angle X‐ray scattering
Motycka, B., Csarman, F., Tscheließnig, R., Hammel, M., & Ludwig, R. (2023) · FEBS Journal · doi:10.1111/febs.16885 · Cited by 3
Implementation of CQA (Critical Quality Attribute) Based Approach for Development of Biosimilars
Gupta, S. K. (2014) · doi:10.1002/9783527673681.ch14 · Cited by 3
Chemical and Genetic Modification
Farys, M., Ginn, C., Badescu, G. O., Peciak, K., Pawlisz, E., Khalili, H., & Brocchini, S. (2013) · Wiley eBooks · doi:10.1002/9780470571224.pse508 · Cited by 3
Considerations for Glycoprotein Production
Clarke, E. C. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3666-4_20 · Cited by 2
Wenzel, E. V., Al-Halabi-Frenzel, L., Demiral, S., Frenzel, A., Gnann, D. C., Keitel, M. C.-E., Lehmler, N., Mukherjee, T., Rauls, J., Schirrmann, T., et al. (2026) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2026.1765764 · Cited by 4
Luo, C., Chen, S., Xu, N., Sai, W., Zhao, W., Li, Y. C., Hu, X. J., Tian, H., Gao, X. D., & Yao, W. B. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.12.085 · Cited by 2
Tevelev, B., Chambers, A., Ghosh, S., Zhang, Y., Marzilli, L. A., Rouse, J. C., Han, S., Moffat, M. A., & Scarcelli, J. J. (2022) · Biotechnology Progress · doi:10.1002/btpr.3320 · Cited by 2
Bennett, C. S., & Nguyen, T.-A. V. (2023) · ACS in focus · doi:10.1021/acsinfocus.7e7027 · Cited by 2
Animal Cell Expression Systems
Butler, M., & Reichl, U. (2017) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2017_31 · Cited by 2
The Glycoform Modifications of sRAGE Matter
Tae, H. J., & Lakatta, E. G. (2013) · Cardiovascular Pharmacology Open Access · doi:10.4172/2329-6607.1000e114 · Cited by 1
Angeletti, A., Bruschi, M., Kajana, X., Lugani, F., Candiano, G., & Ghiggeri, G. M. (2022) · Journal of the American Society of Nephrology · doi:10.1681/asn.2022070755 · Cited by 2
Yoshimura, T., Horiuchi, K., Shimonishi, N., Ogiwara, K., Horie, K., Shima, M., & Nogami, K. (2022) · International Journal of Hematology · doi:10.1007/s12185-022-03468-9 · Cited by 2
Understanding the presence of xeno-derived neu5gc in the human body, and its significance: a review
Pan, S. Y., Anjum, C. E., Chia, Y. C., Kour, A. K., Adalsteinsson, Ö., Papacharalampous, M., Zocchi, M. L., Kimura, I., Sharma, R., Macheret, L., et al. (2020) · Journal of Stem Cell Research & Therapeutics · doi:10.15406/jsrt.2020.06.00144 · Cited by 2
Molecular farming on rescue of pharma industry for next generationsPreprint
Moustafa, K., & Trémouillaux‐Guiller, J. (2018) · doi:10.31221/osf.io/37d9s · Cited by 2
On the Importance of Considering Glycosylation When Evaluating Biologic Therapies
Lemaire, M. J. (2022) · Journal of the American Society of Nephrology · doi:10.1681/asn.2022040461 · Cited by 2
Thomas, P. A., Peele, E. E., Yopak, K. E., Sulikowski, J. A., & Kinsey, S. T. (2024) · Journal of Morphology · doi:10.1002/jmor.21698 · Cited by 1
Iturraspe, F., Bürgi, M., Fuster, R. G., Kratje, R. B., Scorticati, C., & Oggero, M. (2025) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2025.103901 · Cited by 1
Lai, M., Gu, R., Shen, J., Shao, T., Yang, B., Mao, J., & Ye, Q. (2026) · Journal of the American Society of Nephrology · doi:10.1681/asn.0000001246 · Cited by 1
In Vivo Secretion of Bispecific Antibodies Recruiting Lymphocytic Effector Cells
Compte, M., Nuñez‐Prado, N., Sanz, L., & Álvarez‐Vallina, L. (2013) · Antibodies · doi:10.3390/antib2030415 · Cited by 1
Development of polyclonal antibodies for the detection of recombinant human erythropoietin
Farias, C. T., Garcia, M. L., Farias, C. V., Seixas, F. K., Collares, T. V., Dellagostin, O. A., & Hartleben, C. P. (2013) · AFRICAN JOURNAL OF BIOTECHNOLOGY · doi:10.5897/ajb2013.12871 · Cited by 1
Movahed, M., Roudkenar, M. H., Bahadori, M., Mohammadipour, M., Jalili, M. A., & Amiri, F. (2017) · Iranian Journal of Science and Technology Transactions A Science · doi:10.1007/s40995-017-0381-z · Cited by 1
Immunogenicity Risks for Naturally Derived Complex Drugs
Rao, R., & Verthelyi, D. I. (2019) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-030-11751-1_13 · Cited by 1
Initial development of biosimilar immune checkpoint blockers using HEK293 cells
Ramos, M. B., de Araújo, A. É. V., Pestana, C. P., Bom, A. P. D. A., Bastos, R., Almeida-Oliveira, A., Neves, P., & da Silva, H. C. (2020) · Protein Expression and Purification · doi:10.1016/j.pep.2020.105596 · Cited by 1
Lindskog, E. K., Fischer, S., Wenger, T., & Schulz, P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-08-100623-8.00006-2 · Cited by 1
Biosynthesis and Function of Glycoconjugates
Bakar, E., Türker, N. P., & Erim, Z. (2023) · Recent advances in biotechnology · doi:10.2174/9789815179422123080009 · Cited by 1
Recombinant protein expression in mammalian cells
Joshi, M., Verma, P., Mago, P., Agrawal, Y., Gunwal, I., Khurana, S., Tanwar, J., Yadav, U., & Yadav, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-98388-4.00008-3 · Cited by 1
A Comparative Review on the Production of Factor VIII in Human and Non-human Hosts
Ghaemi, A., Moghimi, H., & Sarrafzadeh, M. (2025) · Current Pharmaceutical Design · doi:10.2174/0113816128327353241121050134 · Cited by 1
Sinaga, D. S., Huang, P.-Y., Huang, C., Lu, C.-A., & Huang, L. (2025) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13549-4 · Cited by 1
PERKEMBANGAN TEKNOLOGI SEL MAMALIA CHINESE HAMSTER OVARY (CHO) UNTUK PRODUKSI OBAT BERBASIS PROTEIN
Santoso, A. (2019) · BERITA BIOLOGI · doi:10.14203/beritabiologi.v18i2.3705 · Cited by 1
N-Glycosylation Profiles of the Green Microalgae Chlorella Zofingiensis
Yaman, M. E., Aladağ, E., Kayılı, H. M., Kadıoğlu, Y., & Salih, B. (2021) · Hacettepe Journal of Biology and Chemistry · doi:10.15671/hjbc.717600 · Cited by 1
Presence of Neu5Gc in Animal-Derived Products. Friend Or Foe?
Anjum, C. E., Chia, Y. C., Chan, M. K., Wong, M. B., & Pan, S. Y. (2020) · Stem Cell & Regenerative Medicine · doi:10.33425/2639-9512.1042 · Cited by 1
Chen, W., Ma, R., Wang, T., & Wang, G. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2022.737970 · Cited by 1
Holland, T., & Fischer, R. (2013) · RWTH Publications (RWTH Aachen) · Cited by 1
Antibody Posttranslational Modifications
Jefferis, R. (2016) · Wiley eBooks · doi:10.1002/9781118940648.ch5 · Cited by 2
Mc Cann, A., Mathy, G., & Malphettes, L. (2018) · BMC Proceedings · doi:10.1186/s12919-018-0097-x · Cited by 1
Expression Systems for Recombinant Biopharmaceutical Production by Mammalian Cells in Culture
Brown, A. J., Kalsi, D., Fernandez‐Martell, A., Cartwright, J., Barber, N., Patel, Y. D., Turner, R., Bryant, C. L., Johari, Y. B., & James, D. C. (2017) · Methods and principles in medicinal chemistry · doi:10.1002/9783527699124.ch13 · Cited by 1
Foley, S. L. (2018) · Research@THEA · Cited by 1
Clonagem e expressão do fator VII de coagulação sanguínea em linhagens celulares humanas
de Freitas, M. C. C. (2016) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2016.tde-05012016-091813
Recent Advances in MALDI-MS Based Quantitative Targeted Glycan Analysis
Kim, K.-J., Kim, Y.-W., Hwang, C.-H., Park, H.-K., Jeong, J. H., & Kim, Y. (2015) · KSBB Journal · doi:10.7841/ksbbj.2015.30.5.230
Emerging Principles for the Therapeutic Exploitation of
Scanlan, C. N., Zitzmann, N., & Dwek, R. A. (2016)
Optimizing the glycosylation of recombinant proteins
Rosenlöcher, J. (2016) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-8398
In situ product recovery of antibodies with a reverse flow diafiltration membrane bioreactor
Meier, K., Büchs, J., & Melin, T. (2015) · RWTH Publications (RWTH Aachen)
Advances in Production of Therapeutic Monoclonal Antibodies
Mahajan, R. V., Chand, S., Singh, M. P., Kestwal, A., & Singh, S. (2019) · Wiley eBooks · doi:10.1002/9781119460053.ch7
Using chemical denaturants to determine aggregation propensity of biopharmaceuticals
Holloway, L. (2019) · Research Explorer (The University of Manchester)
Towards the cell-free expression of glycoproteins
Exley, K. (2017) · Spiral (Imperial College London) · doi:10.25560/68742
Bhogal, B. S., Royal, D., Boer, R., & Knight, A. (2020) · Journal of Stem Cell Research & Therapy
Mthembu, Y. (2020) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Braasch, K. (2013) · Mspace (University of Manitoba)
An Oral Vaccine for TGEV Immunization of Pigs
Rajan, V. (2014) · Biotechnology in agriculture and forestry · doi:10.1007/978-3-662-43836-7_8
Spearman, M. A., Lattová, E., Perreault, H., & Butler, M. (2018) · Wiley eBooks · doi:10.1002/9781119378341.ch3
Metadata
- Authors
- Ghaderi, D., Zhang, M., Hurtado-Ziola, N., & Varki, A.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Varki, Ajit
- Venue
- Biotechnology and Genetic Engineering Reviews
- Publisher
- Informa UK Limited
- Published
- 2012-01
- Volume
- 28
- Issue
- 1
- Pages
- 147-176
- ISSN
- 0264-8725 (ISSN-L)
- 2046-5556
- OpenAlex
- W1997984454
- Cited by
- 320
- References
- 128
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 15 · 2023: 13 · 2022: 22 · 2021: 29 · 2020: 29 · 2019: 30 · 2018: 25 · 2017: 30 · 2016: 24 · 2015: 36 · 2014: 23 · 2013: 21 · 2012: 3
- FWCI
- 10.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biotechnology and Genetic Engineering Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- N-glycolylneuraminic acid, alpha-gal epitope, therapeutic glycoproteins, biologic therapy, N-glycosylation, immunogenicity, sialic acid, monoclonal antibodies
- MeSH terms
- Animals, Antibodies, Monoclonal, Epitopes, Biotechnology, Carbohydrate Sequence, Cattle, Cells, Cultured, Culture Media, Disaccharides, Glycoproteins, Glycosylation, Cricetinae, Humans, Insecta, Rabbits, Recombinant Proteins, Sialic Acids, Swine, Cell Culture Techniques, Mice
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