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. 2021 Jun 21;11:12969. doi: 10.1038/s41598-021-92320-x

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Impact of overexpressing individual human glycosyltransferases on growth, productivity and N-linked glycosylation of antibodies produced in stably transfected CHO cell pools. All stable pools were generated via RMCE. The control (Ctrl) pool expressed only IgG1 rituximab LC, HC and DsRed genes. Each of the other 42 stable pools co-expressed IgG1 rituximab genes, a specific human glycosyltransferase gene and DsRed. (A) RT-PCR analysis of human glycosyltransferase transcripts in different stable pools. β-actin (ACT) was used as an internal control. (B–C) Relative change in the integrated viable cell density (IVCD) and specific productivity (qP) in each stably transfected pool to the control. (D–E) Aligned HILIC chromatograms of N-linked glycans on antibodies in the control and representative stable pools which exhibited changes in the N-glycan profiles. Symbolic representation of the N-glycan structures was depicted for dominant peaks. Red dotted line indicated the N-glycan structures that were only found in MGAT3 sample. (F–J) Relative distribution of fucosylation, galactosylation, tri-antennary, sialylation and high-mannose on antibodies produced in different stable pools.

Impact of overexpressing individual human glycosyltransferases on growth, productivity and N-linked glycosylation of antibodies produced in stably transfected CHO cell pools. All stable pools were generated via RMCE. The control (Ctrl) pool expressed only IgG1 rituximab LC, HC and DsRed genes. Each of the other 42 stable pools co-expressed IgG1 rituximab genes, a specific human glycosyltransferase gene and DsRed. (A) RT-PCR analysis of human glycosyltransferase transcripts in different stable pools. β-actin (ACT) was used as an internal control. (B–C) Relative change in the integrated viable cell density (IVCD) and specific productivity (qP) in each stably transfected pool to the control. (D–E) Aligned HILIC chromatograms of N-linked glycans on antibodies in the control and representative stable pools which exhibited changes in the N-glycan profiles. Symbolic representation of the N-glycan structures was depicted for dominant peaks. Red dotted line indicated the N-glycan structures that were only found in MGAT3 sample. (F–J) Relative distribution of fucosylation, galactosylation, tri-antennary, sialylation and high-mannose on antibodies produced in different stable pools.