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The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line
Open accessAbstract
Since 1987, immortalized cells from the ovary of a Chinese hamster have been the workhorse for producing recombinant therapeutics, including monoclonal antibodies, blood factors, hormones, growth factors and enzymes. Xu et al. provide the genome sequence of the ancestral CHO-K1 cell line, which should aid in the optimization of current production cell lines. Chinese hamster ovary (CHO)–derived cell lines are the preferred host cells for the production of therapeutic proteins. Here we present a draft genomic sequence of the CHO-K1 ancestral cell line. The assembly comprises 2.45 Gb of genomic sequence, with 24,383 predicted genes. We associate most of the assembled scaffolds with 21 chromosomes isolated by microfluidics to identify chromosomal locations of genes. Furthermore, we investigate genes involved in glycosylation, which affect therapeutic protein quality, and viral susceptibility genes, which are relevant to cell engineering and regulatory concerns. Homologs of most human glycosylation-associated genes are present in the CHO-K1 genome, although 141 of these homologs are not expressed under exponential growth conditions. Many important viral entry genes are also present in the genome but not expressed, which may explain the unusual viral resistance property of CHO cell lines. We discuss how the availability of this genome sequence may facilitate genome-scale science for the optimization of biopharmaceutical protein production.
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“The availability of genomic sequences has enabled CHO cell engineering with unprecedented precision using engineered nucleases, including zinc finger nucleases (ZFNs) and transcription activator like nucleases (TALENs) and the clustered regularly interspaced short palindromic repeats (CRISPR) system [71–73,75,76].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [71]
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“CHO cells do not express alpha-1,3-galactosyltransferases, which produce the immunogenic alpha-galactosyl epitope (although they have the gene), and the expression of CMP-N-acetylneuraminic acid hydroxylase, which produces CMP-NeuGc, is virtually absent [27,71,72].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [71]
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“Advances in various omics technologies have significantly improved our understanding of CHO cells at different levels and enabled the rational targeting of glycosylation effectors for improved biopharmaceutical production [27,71,72,150–152].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [71]
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Citations
Cites
Initial sequencing and comparative analysis of the mouse genome
Mouse Genome Sequencing Consortium (2002) · Nature · doi:10.1038/nature01262 · Cited by 7,187
De novo assembly of human genomes with massively parallel short read sequencing
Li, R., Zhu, H., Ruan, J., Qian, W., Fang, X., Shi, Z., Li, Y., Li, S., Shan, G., Kristiansen, K., et al. (2010) · Genome Research · doi:10.1101/gr.097261.109 · Cited by 2,926
Self-citationGenome sequence of the Brown Norway rat yields insights into mammalian evolution
Gibbs, R. A., Weinstock, G. M., Metzker, M. L., Muzny, D. M., Sodergren, E. J., Scherer, S. E., Scott, G., Steffen, D. L., Worley, K. C., Burch, P. E., et al. (2004) · Nature · doi:10.1038/nature02426 · Cited by 2,170
Production of recombinant protein therapeutics in cultivated mammalian cells
Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032 · cited 9×
“This is consistent with the observation that CHO cells do not normally show ST6Gal activity19, whereas terminal α(2,3)-linked sialic acid residues are abundant.”
InfluentialAssembly algorithms for next-generation sequencing data
Miller, J. R., Koren, S., & Sutton, G. G. (2010) · Genomics · doi:10.1016/j.ygeno.2010.03.001 · Cited by 1,186
Metabolic engineering of Escherichia coli for direct production of 1,4-butanediol
Yim, H. H., Haselbeck, R. J., Niu, W., Pujol-Baxley, C., Burgard, A. P., Boldt, J., Khandurina, J., Trawick, J. D., Osterhout, R. E., Stephen, R., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.580 · Cited by 1,114
The role of sialic acid in determining the survival of glycoproteins in the circulation
Morell, A. G., Gregoriadis, G., Scheinberg, I. H., Hickman, J., & Ashwell, G. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)76994-4 · Cited by 1,072
A Novel Role for 3-O-Sulfated Heparan Sulfate in Herpes Simplex Virus 1 Entry
Shukla, D., Liu, J., Blaiklock, P., Shworak, N. W., Bai, X., Esko, J. D., Cohen, G. H., Eisenberg, R. J., ROSENBERG, R. D., & Spear, P. G. (1999) · Cell · doi:10.1016/s0092-8674(00)80058-6 · Cited by 1,053
Post-translational modifications in the context of therapeutic proteins
Walsh, G., & Jefferis, R. (2006) · Nature Biotechnology · doi:10.1038/nbt1252 · Cited by 1,007 · cited 1×
“For some of these proteins, differential glycosylation can substantially affect functional activity and/or in vivo circulatory half-lif”
Annotation, submission and screening of repetitive elements in Repbase: RepbaseSubmitter and Censor
Kohany, O., Gentles, A. J., Hankus, L., & Jurka, J. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-474 · Cited by 897
Flagged first, then by citations
1 of the 53 references couldn’t be matched to a known paper.
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Items 401–500 of 786
Expanding the Chinese hamster ovary cell long noncoding RNA transcriptome using RNASeq
Motheramgari, K., Curell, R. V., Tzani, I., Gallagher, C., Castro‐Rivadeneyra, M., Zhang, L., Barron, N., & Clarke, C. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27467 · Cited by 15
A Stable CHO K1 Cell Line for Producing Recombinant Monoclonal Antibody Against TNF-α
Gupta, K., Modi, D. N., Jain, R. D., & Dandekar, P. P. (2021) · Molecular Biotechnology · doi:10.1007/s12033-021-00329-4 · Cited by 15
Hackl, M., Jadhav, V., Klanert, G., Karbiener, M., Scheideler, M., Grillari, J., & Borth, N. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2013.12.018 · Cited by 21
Shin, J., Lee, N., Song, Y., Park, J., Kang, T. J., Kim, S. C., Lee, G. M., & Byung-Kwan, C. (2015) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-015-0233-7 · Cited by 16
Zeh, N., Schlossbauer, P., Raab, N., Klingler, F., Handrick, R., & Otte, K. (2021) · Metabolic Engineering Communications · doi:10.1016/j.mec.2021.e00181 · Cited by 15
Improving expression of recombinant human IGF‐1 using IGF‐1R knockout CHO cell lines
Romand, S., Jostock, T., Fornaro, M., Schmidt, J., Ritter, A., Wilms, B., & Laux, H. (2015) · Biotechnology and Bioengineering · doi:10.1002/bit.25877 · Cited by 15
Toktay, Y., Dayanc, B., & Şentürk, Ş. (2022) · Scientific Reports · doi:10.1038/s41598-022-09887-2 · Cited by 14
The potential of emerging sub-omics technologies for CHO cell engineering
Jerabek, T., Keysberg, C., & Otte, K. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2022.107978 · Cited by 14
Min, H., Kim, S. M., Kim, D., Lee, S., Lee, S., & Lee, J. S. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.977193 · Cited by 14
Proteomics analysis of altered cellular metabolism induced by insufficient copper level
Kang, S., Xiao, G., Ren, D., Zhang, Z., Le, N., Trentalange, M., Gupta, S., Lin, H. C., & Bondarenko, P. V. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.08.001 · Cited by 14
Wingens, M., Gätgens, J., Schmidt, A., Albaum, S. P., Büntemeyer, H., Noll, T., & Hoffrogge, R. (2015) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2015.01.005 · Cited by 15
Heffner, K. M., Hızal, D. B., Kumar, A., Shiloach, J., Zhu, J., Bowen, M. A., & Betenbaugh, M. J. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.06.006 · Cited by 14
Self-citationCao, Y., Kimura, S., Itoi, T., Honda, K., Ohtake, H., & Ōmasa, T. (2011) · Methods · doi:10.1016/j.ymeth.2011.11.002 · Cited by 15
The ‘Omics Revolution in CHO Biology: Roadmap to Improved CHO Productivity
Dahodwala, H., & Sharfstein, S. T. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6972-2_10 · Cited by 14
Tossolini, I., López-Díaz, F. J., Kratje, R. B., & Prieto, C. C. (2018) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2018.09.007 · Cited by 14
Current views on N-glycolylneuraminic acid in therapeutic recombinant proteins
Mastrangeli, R., Audino, M. C., Palinsky, W., Broly, H., & Bierau, H. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.08.004 · Cited by 14
Reciprocal Translocation Observed in End-of-Production Cells of a Commercial CHO-Based Process.
Rouiller, Y., Kleuser, B., Toso, E., Palinsky, W., Rossi, M., Rossatto, P., Barberio, D., & Broly, H. (2015) · PubMed · doi:10.5731/pdajpst.2015.01063 · Cited by 14
Annotation of additional evolutionary conserved microRNAs in CHO cells from updated genomic data
Diendorfer, A. B., Hackl, M., Klanert, G., Jadhav, V., Reithofer, M., Stiefel, F., Hesse, F., Grillari, J., & Borth, N. (2015) · Biotechnology and Bioengineering · doi:10.1002/bit.25539 · Cited by 14
Peng, J., Zhao, Y., Hong, Y., Burkhalter, R. S., Hogue, C. L., Tran, E., Wei, L., Romeo, L. E., Dolley-Sonneville, P., Melkoumian, Z. K., et al. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b05102 · Cited by 15
Nguyen, H. X., Kirkton, R. D., & Bursac, N. (2018) · Nature Protocols · doi:10.1038/nprot.2018.016 · Cited by 14
Key Challenges in Designing CHO Chassis Platforms
Hamdi, A., Széliová, D., Ruckerbauer, D. E., Rocha, I., Borth, N., & Zanghellini, J. (2020) · Processes · doi:10.3390/pr8060643 · Cited by 16
Chen, Y., & Betenbaugh, M. J. (2023) · Metabolic Engineering · doi:10.1016/j.ymben.2023.02.010 · Cited by 13
Self-citationDetection of host cell microprotein impurities in antibody drug products
Tzani, I., Castro‐Rivadeneyra, M., Kelly, P. S., Strasser, L., Zhang, L., CLYNES, M. M., Karger, B. L., Barron, N., Bones, J., Clarke, C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51870-0 · Cited by 14
Toward genome-scale models of the Chinese hamster ovary cells: incentives, status and perspectives
Kaas, C. S., Fan, Y., Weilguny, D., Kristensen, C., Kildegaard, H. F., & Andersen, M. R. (2014) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.14.54 · Cited by 13
Self-citationQiu, H., Gołas, A., Grzmil, P., & Wojnowski, L. (2013) · Journal of Molecular Evolution · doi:10.1007/s00239-013-9585-9 · Cited by 13
Templeton, N., & Young, J. D. (2018) · Biochemical Engineering Journal · doi:10.1016/j.bej.2018.04.008 · Cited by 13
Lin, P., Liu, R., Alvin, K., Shahreel, W., Murgolo, N., Ye, J., Du, Z., & Song, Z. (2020) · Biotechnology Journal · doi:10.1002/biot.202000267 · Cited by 13
Klingler, F., Mathias, S., Schneider, H., Buck, T., Raab, N., Zeh, N., Shieh, Y., Pfannstiel, J., & Otte, K. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27811 · Cited by 15
“…have been studied in great detail using OMICs analyses to facilitate sophisticated approaches for cell line development (Baycin‐Hizal et al., 2012; Farrell et al., 2014; Henry et al., 2017; Kumar et al., 2015; Lewis et al., 2013; Nissom et al., 2006; Sommeregger et al., 2016; Xu et al., 2011).”
dos Reis, V. P., Keller, M., Schmidt, K., Ulrich, R. G., & Groschup, M. H. (2021) · Viruses · doi:10.3390/v14010018 · Cited by 13
Williamson, J., Miller, J., McLaughlin, J. F., Combs, R. G., & Chu, C. H. (2018) · Biotechnology Progress · doi:10.1002/btpr.2662 · Cited by 16
Arylamine N‐Acetyltransferases
Svensson, C. K., & Sim, E. (2002) · Wiley eBooks · doi:10.1002/0471203076.emm0321 · Cited by 13
Recombinant Protein Expression and Its Biotechnological Applications in Chlorella spp.
Chen, C., & Ward, V. C. A. (2024) · SynBio · doi:10.3390/synbio2020013 · Cited by 13
Bryan, L., Henry, M., Kelly, R. M., Frye, C., Osborne, M., Clynes, M., & Meleady, P. (2021) · BMC Biotechnology · doi:10.1186/s12896-021-00704-8 · Cited by 12
Chen, S., Yang, F., Zhu, Z., Cao, W., Lian, K., Zhang, W. Y., Zhu, Z., He, J., Guo, J., Liu, X., et al. (2022) · Veterinary Microbiology · doi:10.1016/j.vetmic.2022.109550 · Cited by 12
Self-citationChitwood, D. G., Wang, Q., Klaubert, S. R., Green, K., Wu, C. H., Harcum, S. W., & Saski, C. A. (2023) · Scientific Reports · doi:10.1038/s41598-023-27962-0 · Cited by 12
LncRNA analysis of mAb producing CHO clones reveals marker and engineering potential
Novak, N., Baumann, M., Friss, A. F., Cairns, V. R., DeMaria, C., & Borth, N. (2023) · Metabolic Engineering · doi:10.1016/j.ymben.2023.05.003 · Cited by 12
Chen, C., Le, H., & Goudar, C. T. (2015) · Biotechnology Progress · doi:10.1002/btpr.2137 · Cited by 12
Nicolae, A., Wahrheit, J., Nonnenmacher, Y., Weyler, C., & Heinzle, E. (2015) · Metabolic Engineering · doi:10.1016/j.ymben.2015.09.014 · Cited by 12
Chen, J., Haverty, J., Deng, L., Li, G., Qiu, P., Liu, Z., & Shi, S. (2013) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2013.07.001 · Cited by 12
Curell, R. V., & Barron, N. (2018) · Biotechnology Journal · doi:10.1002/biot.201700220 · Cited by 14
Tossolini, I., Gugliotta, A., Díaz, F. L., Kratje, R. B., & Prieto, C. C. (2022) · Plasmid · doi:10.1016/j.plasmid.2022.102620 · Cited by 12
Suto, Y., Akiyama, M., Gotoh, T., & Hirai, M. (2013) · CYTOLOGIA · doi:10.1508/cytologia.78.97 · Cited by 12
Becker, J. S., Timmermann, C., Rupp, O., Albaum, S. P., Brinkrolf, K., Goesmann, A., Pühler, A., Tauch, A., & Noll, T. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.02.021 · Cited by 12
Augmenting Chinese hamster genome assembly by identifying regions of high confidence
Vishwanathan, N., Bandyopadhyay, A. A., Fu, H., Sharma, M., Johnson, K. C., Mudge, J., Ramaraj, T., Onsongo, G., Silverstein, K. A. T., Jacob, N. M., et al. (2016) · Biotechnology Journal · doi:10.1002/biot.201500455 · Cited by 12
Wippermann, A., & Noll, T. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.08.005 · Cited by 12
Sam, N. T., Misaki, R., Ohashi, T., & Fujiyama, K. (2018) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2018.01.010 · Cited by 12
Tamošaitis, L., & Smales, C. M. (2018) · Biotechnology Journal · doi:10.1002/biot.201800066 · Cited by 12
Christensen, M. D., Nitiyanandan, R., Meraji, S., Daer, R., Godeshala, S., Goklany, S., Haynes, K. A., & Rege, K. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.06.030 · Cited by 12
“79%) of repetitious elements compared to human cells (46%) [24], and overrepresentation of translation, metabolism and protein modification-related gene functions [24].”
Baek, E. H., Lee, J. S., & Lee, G. M. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26777 · Cited by 12
Duroy, P., Bosshard, S., Schmid‐Siegert, E., Neuenschwander, S., Arib, G., Mercier, P. L., Masternak, J., Roesch, L., Buron, F., Girod, P., et al. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.27200 · Cited by 13
“The CHO‐K1 genome assemblies were from published databases of the Chinese hamster genome assembly (NCBI CHO‐K1 reference genome; X. Xu et al., 2011) and from sequencing data performed on an RSII (Pacific Biosciences) using a total of 197 SMRT cells.”
MacDonald, M. L., Polson, S. W., & Lee, K. H. (2021) · mSphere · doi:10.1128/msphere.01336-20 · Cited by 11
Self-citationGeisler, C. (2018) · BMC Biotechnology · doi:10.1186/s12896-017-0412-z · Cited by 12
Schulz, A., Munro, T. P., Puklowski, A., Slack, E. M. C., Tolstrup, A. B., & Otte, K. (2026) · mAbs · doi:10.1080/19420862.2026.2615475 · Cited by 14
Amino acid degradation pathway inhibitory by‐products trigger apoptosis in CHO cells
Martínez, V. S., Rodríguez, K., McCubbin, T., Tong, J., Mahler, S. M., Shave, E., Baker, K. N., Munro, T. P., & Marcellin, E. (2024) · Biotechnology Journal · doi:10.1002/biot.202300338 · Cited by 14
McClenahan, S. D., Uhlenhaut, C., & Krause, P. R. (2014) · Vaccine · doi:10.1016/j.vaccine.2014.10.022 · Cited by 11
Lawrence, P., Pacheco, J. M., Stenfeldt, C., Arzt, J., Rai, D. K., & Rieder, E. A. (2016) · Virology · doi:10.1016/j.virol.2016.02.004 · Cited by 11
Identifying a robust design space for glycosylation during monoclonal antibody production
Amand, M. M. S., Hayes, J., Radhakrishnan, D., Fernandez, J., Meyer, B., Robinson, A. S., & Ogunnaike, B. A. (2016) · Biotechnology Progress · doi:10.1002/btpr.2316 · Cited by 11
Gowtham, Y. K., Saski, C. A., & Harcum, S. W. (2017) · Biotechnology Progress · doi:10.1002/btpr.2462 · Cited by 13
Ota, F., Kizuka, Y., Nakano, M., Yamaguchi, Y., Kitazume, S., Ookawara, T., & Taniguchi, N. (2017) · Glycobiology · doi:10.1093/glycob/cwx087 · Cited by 11
Lai, Z., Choudhury, F. K., Tang, D., Liang, X., Dean, B., Misaghi, S., & Sangaraju, D. (2022) · Biomedical Chromatography · doi:10.1002/bmc.5348 · Cited by 11
Challenges and Emerging Technologies in Biomanufacturing of Monoclonal Antibodies (mAbs)
McDonnell, S., Principe, R. F., Zamprognio, M. S., & Whelan, J. (2022) · Biomedical engineering · doi:10.5772/intechopen.108565 · Cited by 11
Ghanbari, S., Bayat, E., Azizi, M., Fard‐Esfahani, P., Modarressi, M. H., & Davami, F. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12322-1 · Cited by 11
Kremkow, B. G., & Lee, K. H. (2013) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.13.52 · Cited by 11
Self-citationRole of epigenetics in expression of recombinant proteins from mammalian cells
Dahodwala, H., & Sharfstein, S. T. (2014) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.14.47 · Cited by 13
Genetic engineering of CHO cells for viral resistance to minute virus of mice
Mascarenhas, J., Korokhov, N., Burger, L. R., Kassim, A., Tuter, J., Miller, D., Borgschulte, T., George, H. J., Chang, A., Pintel, D. J., et al. (2016) · Biotechnology and Bioengineering · doi:10.1002/bit.26186 · Cited by 11
Sathasivam, R., Guo, R., Wang, H., Lim, W., & Ki, J. (2018) · Journal of Applied Phycology · doi:10.1007/s10811-018-1445-y · Cited by 11
Subphysiological temperature induces pervasive alternative splicing in Chinese hamster ovary cells
Tzani, I., Monger, C., Motheramgari, K., Gallagher, C., Hagan, R., Kelly, P. S., Costello, A., Meiller, J., Floris, P., Zhang, L., et al. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27365 · Cited by 11
Regulatory Elements in Vectors for Efficient Generation of Cell Lines Producing Target Proteins
Maksimenko, O. G., Gasanov, N. B., & Georgiev, P. G. (2015) · Acta Naturae · doi:10.32607/20758251-2015-7-3-15-26 · Cited by 11
He, L., Desai, J., Gao, J., Hazeltine, L. B., Lian, Z., Calley, J. N., & Frye, C. C. (2018) · Biotechnology Journal · doi:10.1002/biot.201700254 · Cited by 11
In pursuit of a minimal CHO genome: Establishment of large-scale genome deletions
Jerabek, T., Weiß, L., Fahrion, H., Zeh, N., Raab, N., Lindner, B., Fischer, S., & Otte, K. (2023) · New Biotechnology · doi:10.1016/j.nbt.2023.12.007 · Cited by 10
Woo, H. J., Kim, J., Kim, S. M., Kim, D., Moon, J. Y., Park, D., & Lee, J. S. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.04.023 · Cited by 10
Kang, J., Lim, S.-J., Kwon, O., Lee, S., Kim, H. H., & Oh, D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133739 · Cited by 10
Bioinformatic analysis of Chinese hamster ovary host cell protein lipases
MacDonald, M. L., Hamaker, N. K., & Lee, K. H. (2018) · AIChE Journal · doi:10.1002/aic.16378 · Cited by 10
Self-citationSchmieder, V., Novak, N., Dhiman, H., Ly, N. N., Serafimova, E., Klanert, G., Baumann, M., Kildegaard, H. F., & Borth, N. (2021) · Biotechnology Reports · doi:10.1016/j.btre.2021.e00649 · Cited by 10
Formation of Oleic Acid Chlorohydrins in Vegetables during Postharvest Chlorine Disinfection
Simpson, A. M.-A., Suh, M.-J., Plewa, M. J., & Mitch, W. A. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.1c04362 · Cited by 10
Hughes, L., Carton, R., Minguzzi, S., McEntee, G., Deinum, E. E., O’Connell, M. J., & Parle‐McDermott, A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.017 · Cited by 10
Toward product attribute control: developments from genome sequencing
Baik, J. Y., & Lee, K. H. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.05.001 · Cited by 10
Self-citationLoreti, N., Ambao, V., Andreone, L., Trigo, R., Bussmann, U. A., & Campo, S. (2012) · Reproduction · doi:10.1530/rep-12-0228 · Cited by 10
High-level expression of recombinant IgG1 by CHO K1 platform
Xu, N., Ou, J., Gilani, A.-K., Zhou, L., & Liu, M. (2015) · Frontiers of Chemical Science and Engineering · doi:10.1007/s11705-015-1531-5 · Cited by 10
“The parental CHO K1 is derived from the first ancestral CHO cell, and other CHO cells are derived from CHO K1 [12,13].”
Zhu, G., Sun, L., Albanetti, T., Linkous, T., Larkin, C. J., Schoner, R. G., McGivney, J. B., & Dovic̀hi, N. J. (2016) · Biotechnology and Bioengineering · doi:10.1002/bit.25991 · Cited by 10
Lectin bio‐layer interferometry for assessing product quality of Fc‐ glycosylated immunoglobulin G
Wallner, J., Sissolak, B., Sommeregger, W., Lingg, N., Striedner, G., & Vorauer‐Uhl, K. (2019) · Biotechnology Progress · doi:10.1002/btpr.2864 · Cited by 10
Kido, M., Idogaki, H., Nishikawa, K., & Ōmasa, T. (2020) · Cytotechnology · doi:10.1007/s10616-020-00434-3 · Cited by 10
Bryan, L., Henry, M., Kelly, R. M., Lloyd, M. E., Frye, C., Osborne, M., Clynes, M., & Meleady, P. (2021) · Current Research in Biotechnology · doi:10.1016/j.crbiot.2021.02.002 · Cited by 8
Visualizing bleb mass dynamics in single cells using quantitative phase microscopy
Steelman, Z. A., Владимировна, С. А., Coker, Z. N., Kiester, A. S., Noojin, G. D., Ibey, B. L., & Bixler, J. N. (2021) · Applied Optics · doi:10.1364/ao.426147 · Cited by 10
From omics to cellular mechanisms in mammalian cell factory development
Samoudi, M., Masson, H. O., Kuo, C., Robinson, C. M., & Lewis, N. E. (2021) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2021.100688 · Cited by 11
Self-citationFischer, S., Mathias, S., Stadermann, A., Yang, S., Schmieder, V., Zeh, N., Schmidt, N., Richter, P., Wright, S., Zimmermann, E., et al. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.28015 · Cited by 10
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Mathew, M. P., Tan, E., Labonte, J. W., Shah, S., Saeui, C. T., Liu, L., Bhattacharya, R., Bovonratwet, P., Gray, J. J., & Yarema, K. J. (2017) · ChemBioChem · doi:10.1002/cbic.201600698 · Cited by 10
Wurm, F. M., & de Jesus, M. (2016) · Wiley eBooks · doi:10.1002/9781118940648.ch11 · Cited by 10
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Sieck, J. B., Schild, C., & von Hagen, J. (2017) · doi:10.1002/9783527699902.ch7 · Cited by 10
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Schaub, J., Ankenbauer, A., Habicher, T., Löffler, M., Maguire, N., Monteil, D. T., Püngel, S., Stepper, L., Stiefel, F., Thoma, J., et al. (2023) · Physical Sciences Reviews · doi:10.1515/psr-2022-0113 · Cited by 10
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Chin, P.-J., Lambert, C., Beurdelay, P., Charlebois, R. L., Colinet, A.-S., Éloit, M., Gilchrist, S., Gilleece, M., Hess, M. C., Leimbach, A., et al. (2025) · npj Vaccines · doi:10.1038/s41541-025-01104-1 · Cited by 9
Self-citationMarco, F. D., Sebastian, I. R., Napoleone, A., Molin, A., Riedl, M., Bydlinski, N., Motheramgari, K., Hussein, M. K., Kramer, L., Kelly, T. J., et al. (2025) · Metabolic Engineering · doi:10.1016/j.ymben.2025.08.007 · Cited by 9
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Le, H., Chen, C., & Goudar, C. T. (2015) · Biotechnology and Bioengineering · doi:10.1002/bit.25649 · Cited by 9
Wijaya, A. W., Verhagen, N., Teleki, A., & Takors, R. (2021) · Engineering in Life Sciences · doi:10.1002/elsc.202100057 · Cited by 8
Mao, L., Schneider, J. W., & Robinson, A. S. (2023) · Biotechnology Journal · doi:10.1002/biot.202300397 · Cited by 10
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Ha, T. K., & Lee, G. M. (2015) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.15.6 · Cited by 9
Chen, C., Le, H., & Goudar, C. T. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26290 · Cited by 9
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Chen, X., Liu, X., Xiao, Z., Liu, J., Zhao, L., Tan, W., & Fan, L. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09850-8 · Cited by 9
Self-citationHigh‐resolution three‐dimensional chromatin profiling of the Chinese hamster ovary cell genome
Bevan, S., Schoenfelder, S., Young, R. J., Zhang, L., Andrews, S. R., Fraser, P., & O'Callaghan, P. M. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27607 · Cited by 9
Metadata
- Authors
- Xu, X., Nagarajan, H., Lewis, N. E., Pan, S., Cai, Z., Liu, X., Chen, W., Xie, M., Wang, W., Hammond, S., Andersen, M. R., Neff, N., Passarelli, B., Koh, W., Fan, H. C., Wang, J., Gui, Y., Lee, K. H., Betenbaugh, M. J., Quake, S. R., Famili, I., Palsson, B. O., & Wang, J.
- Affiliations
- BGI Group (China) (CN)
- Peking University Shenzhen Hospital (CN)
- Delaware Biotechnology Institute (US)
- Technical University of Denmark (DK)
- Howard Hughes Medical Institute (US)
- Johns Hopkins University (US)
- Corresponding author
- Wang, Jianbin
- Wang, Jun
- ORCID
- Venue
- Nature Biotechnology
- Published
- 2011-08
- Volume
- 29
- Issue
- 8
- Pages
- 735-741
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- PMC
- PMC3164356
- OpenAlex
- W2093343938
- Cited by
- 785
- References
- 53
- Citations by year
- 2026: 22 · 2025: 25 · 2024: 37 · 2023: 35 · 2022: 39 · 2021: 58 · 2020: 38 · 2019: 45 · 2018: 78 · 2017: 57 · 2016: 59 · 2015: 77 · 2014: 79 · 2013: 64 · 2012: 53
- FWCI
- 27.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Biotechnology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion)
- Funders
- Novo Nordisk Fonden (NNF10CC1016517)
- National Cancer Institute (R44CA139977)
- National Center for Research Resources (P20RR016472)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- CHO-K1 cells, CHO cells, draft genome sequence, therapeutic protein production, monoclonal antibodies, virus resistance, cell line engineering, genome assembly, gene expression
- MeSH terms
- Animals, Chromosome Mapping, Cricetulus, Glycosylation, Cricetinae, Models, Biological, Molecular Sequence Data, CHO Cells, Genome, Sequence Analysis, DNA, Genomics
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