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Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells

Immunoglobulin A (IgA) has been showing potential as a new therapeutic antibody. However, recombinant IgA suffers from low yield. Supplementation of the medium is an effective approach to improving the production and quality of recombinant proteins. In this study, we adapted IgA1-producing CHO-K1 su...

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Autores principales: Choa, John Benson D., Sasaki, Tadahiro, Kajiura, Hiroyuki, Ikuta, Kazuyoshi, Fujiyama, Kazuhito, Misaki, Ryo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10018586/
https://www.ncbi.nlm.nih.gov/pubmed/37163134
http://dx.doi.org/10.1007/s10616-023-00571-5
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author Choa, John Benson D.
Sasaki, Tadahiro
Kajiura, Hiroyuki
Ikuta, Kazuyoshi
Fujiyama, Kazuhito
Misaki, Ryo
author_facet Choa, John Benson D.
Sasaki, Tadahiro
Kajiura, Hiroyuki
Ikuta, Kazuyoshi
Fujiyama, Kazuhito
Misaki, Ryo
author_sort Choa, John Benson D.
collection PubMed
description Immunoglobulin A (IgA) has been showing potential as a new therapeutic antibody. However, recombinant IgA suffers from low yield. Supplementation of the medium is an effective approach to improving the production and quality of recombinant proteins. In this study, we adapted IgA1-producing CHO-K1 suspension cells to a high concentration (150 mM) of different disaccharides, namely sucrose, maltose, lactose, and trehalose, to improve the production and quality of recombinant IgA1. The disaccharide-adapted cell lines had slower cell growth rates, but their cell viability was extended compared to the nonadapted IgA1-producing cell line. Glucose consumption was exhausted in all cell lines except for the maltose-adapted one, which still contained glucose even after the 9th day of culturing. Lactate production was higher among the disaccharide-adapted cell lines. The specific productivity of the maltose-adapted IgA1-producing line was 4.5-fold that of the nonadapted line. In addition, this specific productivity was higher than in previous productions of recombinant IgA1 with a lambda chain. Lastly, secreted IgA1 aggregated in all cell lines, which may have been caused by self-aggregation. This aggregation was also found to begin inside the cells for maltose-adapted cell line. These results suggest that a high concentration of disaccharide-supplemented induced hyperosmolarity in the IgA1-producing CHO-K1 cell lines. In addition, the maltose-adapted CHO-K1 cell line benefited from having an additional source of carbohydrate. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10616-023-00571-5.
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spelling pubmed-100185862023-03-16 Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells Choa, John Benson D. Sasaki, Tadahiro Kajiura, Hiroyuki Ikuta, Kazuyoshi Fujiyama, Kazuhito Misaki, Ryo Cytotechnology Research Immunoglobulin A (IgA) has been showing potential as a new therapeutic antibody. However, recombinant IgA suffers from low yield. Supplementation of the medium is an effective approach to improving the production and quality of recombinant proteins. In this study, we adapted IgA1-producing CHO-K1 suspension cells to a high concentration (150 mM) of different disaccharides, namely sucrose, maltose, lactose, and trehalose, to improve the production and quality of recombinant IgA1. The disaccharide-adapted cell lines had slower cell growth rates, but their cell viability was extended compared to the nonadapted IgA1-producing cell line. Glucose consumption was exhausted in all cell lines except for the maltose-adapted one, which still contained glucose even after the 9th day of culturing. Lactate production was higher among the disaccharide-adapted cell lines. The specific productivity of the maltose-adapted IgA1-producing line was 4.5-fold that of the nonadapted line. In addition, this specific productivity was higher than in previous productions of recombinant IgA1 with a lambda chain. Lastly, secreted IgA1 aggregated in all cell lines, which may have been caused by self-aggregation. This aggregation was also found to begin inside the cells for maltose-adapted cell line. These results suggest that a high concentration of disaccharide-supplemented induced hyperosmolarity in the IgA1-producing CHO-K1 cell lines. In addition, the maltose-adapted CHO-K1 cell line benefited from having an additional source of carbohydrate. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10616-023-00571-5. Springer Netherlands 2023-03-16 2023-06 /pmc/articles/PMC10018586/ /pubmed/37163134 http://dx.doi.org/10.1007/s10616-023-00571-5 Text en © The Author(s), under exclusive licence to Springer Nature B.V. 2023, Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
spellingShingle Research
Choa, John Benson D.
Sasaki, Tadahiro
Kajiura, Hiroyuki
Ikuta, Kazuyoshi
Fujiyama, Kazuhito
Misaki, Ryo
Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells
title Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells
title_full Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells
title_fullStr Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells
title_full_unstemmed Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells
title_short Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells
title_sort effects of various disaccharide adaptations on recombinant iga1 production in cho-k1 suspension cells
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10018586/
https://www.ncbi.nlm.nih.gov/pubmed/37163134
http://dx.doi.org/10.1007/s10616-023-00571-5
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