Multiplex secretome engineering enhances recombinant protein production and purity

Autor: Stefan Kol, Daniel Ley, Tune Wulff, Marianne Decker, Johnny Arnsdorf, Sanne Schoffelen, Anders Holmgaard Hansen, Tanja Lyholm Jensen, Jahir M. Gutierrez, Austin W. T. Chiang, Helen O. Masson, Bernhard O. Palsson, Bjørn G. Voldborg, Lasse Ebdrup Pedersen, Helene Faustrup Kildegaard, Gyun Min Lee, Nathan E. Lewis

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)

Host cell proteins can contaminate biotherapeutics and compromise and degrade their quality. Here the authors use modelling and CRISPR to delete secreted host proteins in CHO cells, leading to improved monoclonal antibody production and purity.

Externí odkaz: https://doaj.org/article/fb48699f0dc94c81a1ca056457c7fde6

A Markov model of glycosylation elucidates isozyme specificity and glycosyltransferase interactions for glycoengineering

Autor: Johnny Arnsdorf, Chenguang Liang, Bjørn G. Voldborg, Benjamin P. Kellman, Bokan Bao, Anders Holmgaard Hansen, Nathan E. Lewis, James T. Sorrentino, Austin W. T. Chiang, Sanne Schoffelen

Publikováno v: Current Research in Biotechnology, Vol 2, Iss, Pp 22-36 (2020)
Liang, C, Chiang, A W T, Hansen, A H, Arnsdorf, J, Schoffelen, S, Sorrentino, J T, Kellman, B P, Bao, B, Voldborg, B G & Lewis, N E 2020, ' A Markov model of glycosylation elucidates isozyme specificity and glycosyltransferase interactions for glycoengineering ', Current Research in Biotechnology, vol. 2, pp. 22-36 . https://doi.org/10.1016/j.crbiot.2020.01.001
Curr Res Biotechnol

Glycosylated biopharmaceuticals are important in the global pharmaceutical market. Despite the importance of their glycan structures, our limited knowledge of the glycosylation machinery still hinders controllability of this critical quality attribut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8804b7be972f26057385ebe88f695122
http://www.sciencedirect.com/science/article/pii/S2590262820300010

Highly Selective Lysine Acylation in Proteins Using a Lys-His Tag Sequence

Autor: Christian Kofoed, Shunliang Wu, Kasper K. Sørensen, Tuule Treiberg, Johnny Arnsdorf, Sara P. Bjørn, Tanja L. Jensen, Bjørn G. Voldborg, Mikkel B. Thygesen, Knud J. Jensen, Sanne Schoffelen

Publikováno v: Kofoed, C, Wu, S, Sørensen, K K, Treiberg, T, Arnsdorf, J, Bjørn, S P, Jensen, T L, Voldborg, B G, Thygesen, M B, Jensen, K J & Schoffelen, S 2022, ' Highly Selective Lysine Acylation in Proteins Using a Lys-His Tag Sequence ', Chemistry: A European Journal, vol. 28, no. 15, e202200147 . https://doi.org/10.1002/chem.202200147
Kofoed, C, Wu, S, Sørensen, K K, Treiberg, T, Arnsdorf, J, Bjørn, S P, Jensen, T L, Voldborg, B G, Thygesen, M B, Jensen, K J & Schoffelen, S 2022, ' Highly selective lysine acylation in proteins using a Lys-His tag sequence ', Chemistry-A European Journal, vol. 28, no. 15 . https://doi.org/10.1002/chem.202200147

Chemical modification of proteins has numerous applications, but it has been challenging to achieve the required high degree of selectivity on lysine amino groups. Recently, we described the highly selective acylation of proteins with an N-terminal G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51595d1281f109d67226de44c10a40e4
https://curis.ku.dk/portal/da/publications/highly-selective-lysine-acylation-in-proteins-using-a-lyshis-tag-sequence(e5726e1f-758b-4b67-9a4d-0598a064138f).html

Glyco-engineered CHO cell lines producing alpha-1-antitrypsin and C1 esterase inhibitor with fully humanized N-glycosylation profiles

Autor: Henning Gram Hansen, Stefan Kol, Gyun Min Lee, Thomas Amann, Mikael Rørdam Andersen, Bjørn G. Voldborg, Saranya Nallapareddy, Johnny Arnsdorf, Helene Faustrup Kildegaard, Anders Holmgaard Hansen

Publikováno v: Amann, T, Hansen, A H, Kol, S, Hansen, H G, Arnsdorf, J, Nallapareddy, S, Voldborg, B, Min Lee, G, Andersen, M R & Kildegaard, H F 2019, ' Glyco-engineered CHO cell lines producing alpha-1-antitrypsin and C1 esterase inhibitor with fully humanized N-glycosylation profiles ', Metabolic Engineering, vol. 52, pp. 143-152 . https://doi.org/10.1016/j.ymben.2018.11.014
Metabolic Engineering

Recombinant Chinese hamster ovary (CHO) cells are able to provide biopharmaceuticals that are essentially free of human viruses and have N-glycosylation profiles similar, but not identical, to humans. Due to differences in N-glycan moieties, two memb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cece00bb07c4cd6c938a535a10108c1c
https://doi.org/10.1016/j.ymben.2018.11.014

Multiplex secretome engineering enhances recombinant protein production and purity

Autor: Bernhard O. Palsson, Austin W. T. Chiang, Johnny Arnsdorf, Marianne Decker, Sanne Schoffelen, Tune Wulff, Lasse Ebdrup Pedersen, Helene Faustrup Kildegaard, Stefan Kol, Tanja Lyholm Jensen, Jahir M. Gutierrez, Gyun Min Lee, Bjørn G. Voldborg, Anders Holmgaard Hansen, Helen O. Masson, Daniel Ley, Nathan E. Lewis

Publikováno v: Nature communications, vol 11, iss 1
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
Kol, S, Ley, D, Wulff, T, Decker, M, Arnsdorf, J, Schoffelen, S, Hansen, A H, Jensen, T L, Gutierrez, J M, Chiang, A W T, Masson, H O, Palsson, B O, Voldborg, B G, Pedersen, L E, Kildegaard, H F, Min Lee, G & Lewis, N E 2020, ' Multiplex secretome engineering enhances recombinant protein production and purity ', Nature Communications, vol. 11, no. 1 . https://doi.org/10.1038/s41467-020-15866-w
Nature Communications

Host cell proteins (HCPs) are process-related impurities generated during biotherapeutic protein production. HCPs can be problematic if they pose a significant metabolic demand, degrade product quality, or contaminate the final product. Here, we pres

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39eafb13b29626fb0af0e6200e0258ea
https://escholarship.org/uc/item/6dr7w8j6