Evidence map›Paper›PMID 34155258›Full record

ArticleScientific reports2021

Multiplexed engineering glycosyltransferase genes in CHO cells via targeted integration for producing antibodies with diverse complex-type N-glycans.

Ngan T B Nguyen, Jianer Lin, Shi Jie Tay, Mariati, Jessna Yeo, Terry Nguyen-Khuong, Yuansheng Yang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 33 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Ngan T B NguyenBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Jianer LinBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Shi Jie TayBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
MariatiBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Jessna YeoBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Terry Nguyen-KhuongBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Yuansheng YangBioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore. yang_yuansheng@bti.a-star.edu.sg.
Agency for Science, Technology and Research · SGBioprocessing Technology Institute · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Therapeutic antibodies are decorated with complex-type N-glycans that significantly affect their biodistribution and bioactivity. The N-glycan structures on antibodies are incompletely processed in wild-type CHO cells due to their limited glycosylation capacity. To improve N-glycan processing, glycosyltransferase genes have been traditionally overexpressed in CHO cells to engineer the cellular N-glycosylation pathway by using random integration, which is often associated with large clonal variations in gene expression levels. In order to minimize the clonal variations, we used recombinase-mediated-cassette-exchange (RMCE) technology to overexpress a panel of 42 human glycosyltransferase genes to screen their impact on antibody N-linked glycosylation. The bottlenecks in the N-glycosylation pathway were identified and then released by overexpressing single or multiple critical genes. Overexpressing B4GalT1 gene alone in the CHO cells produced antibodies with more than 80% galactosylated bi-antennary N-glycans. Combinatorial overexpression of B4GalT1 and ST6Gal1 produced antibodies containing more than 70% sialylated bi-antennary N-glycans. In addition, antibodies with various tri-antennary N-glycans were obtained for the first time by overexpressing MGAT5 alone or in combination with B4GalT1 and ST6Gal1. The various N-glycan structures and the method for producing them in this work provide opportunities to study the glycan structure-and-function and develop novel recombinant antibodies for addressing different therapeutic applications.

Indexed as

Protein EngineeringAnimalsAntibody FormationCell Culture TechniquesCHO CellsCricetulusGene ExpressionGlycosylationGlycosyltransferasesHumansPlasmidsPolysaccharidesRecombinant ProteinsGlycosyltransferasesPolysaccharidesRecombinant Proteins

Identifiers

PMID34155258
PMCPMC8217518
OpenAlexW3176516862

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.