Zinc supplementation decreases galactosylation of recombinant IgG in CHO cells

Applied Microbiology and Biotechnology
Anuja PrabhuMugdha Gadgil

Abstract

Trace element composition of culture medium can be altered to modulate glycoform of recombinant glycoproteins. In this study, we show that Zn2+ supplementation at or above 100 μM decreases galactosylation of recombinant IgG expressed in Chinese Hamster Ovary cells. This decrease in galactosylation is not due to reduced galactosyltransferase expression. This effect persists upon supplementation of galactose and uridine to the culture, indicating that it may not be due to reduced UDP-Gal availability. Measurements of galactosyltransferase activity in the cell lysate show that activity decreases with increasing Zn2+/Mn2+ ratio. This suggests that one possible explanation of the effect of Zn2+ may be reduced intracellular galactosyltransferase activity due to increase in Zn2+/Mn2+ ratio. Consistent with this, the decrease in galactosylation of IgG could be reversed by supplementation of Mn2+ (a cofactor of galactosyltransferase) which increases intracellular Mn2+ content. Measurement of total intracellular Zn2+ content, however, indicates no significant upregulation of total intracellular Zn2+ content and no significant downregulation of intracellular Mn2+ content with Zn2+ supplementation. One possible explanation could be that ce...Continue Reading

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Citations

Dec 21, 2019·Applied Microbiology and Biotechnology·Ryan J GrahamChikkathur N Madhavarao
Oct 18, 2018·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Anuja Prabhu, Mugdha Gadgil
Aug 10, 2019·Cytotechnology·Berta Capella RocaMartin Clynes
Jul 4, 2020·Trends in Biotechnology·Renato MastrangeliHorst Bierau
Apr 2, 2021·Frontiers in Bioengineering and Biotechnology·Weifeng LiTian-Yun Wang

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Methods Mentioned

BETA
glycosylation
enzyme-linked immunosorbent assay

Software Mentioned

Agilent Chem Station

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