Evidence map›Paper›PMID 40817708›Full record

ArticleBiotechnology and bioengineering2025

Genetic Divergence and Antibody Expression Influence the N-Glycomes of CHO-K1 and CHO-S Cells.

Roberto Donini, Pat Blundell, Richard J Pleass, Dongli Lu, Anne Dell, Cleo Kontoravdi, Stuart M Haslam

Abstract read
In one paragraph

Article in Biotechnology and bioengineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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.

Roberto DoniniDepartment of Life Sciences, Imperial College London, London, UK.ORCID https://orcid.org/0000-0001-5270-2854
Pat BlundellDepartment of Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool, UK.ORCID https://orcid.org/0000-0003-3386-5660
Richard J PleassDepartment of Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool, UK.ORCID https://orcid.org/0000-0001-7438-8296
Dongli LuDepartment of Life Sciences, Imperial College London, London, UK.
Anne DellDepartment of Life Sciences, Imperial College London, London, UK.ORCID https://orcid.org/0000-0003-1380-2347
Cleo KontoravdiDepartment of Chemical Engineering, Imperial College London, London, UK.ORCID https://orcid.org/0000-0003-0213-4830
Stuart M HaslamDepartment of Life Sciences, Imperial College London, London, UK.ORCID https://orcid.org/0000-0002-5563-679X

Funding

R.D. thanks the U.K. Biotechnology and Biological Sciences Research Council (BBSRC) for their PhD studentship (BB/M011178/1). R.J.P. was funded by a Wellcome Trust Innovator Award GRANT_NUMBER: 208938/Z/17/Z and UKRI MRC CIC Awards CiVC 2017-18 (MC_PC_17167).Wellcome Trust
6 · The paper itself

Abstract

While Chinese hamster ovary (CHO) cells continue to be the workhorse of recombinant therapeutic protein production, decades of genetic divergence in the industrially relevant CHO-K1 and CHO-S cell lines, are likely to have resulted in differing glycosylation capabilities. Glycosylation can influence the efficacy, serum half-life, and safety of biologics, and as a critical quality attribute of glycoprotein biopharmaceuticals, it is essential to better understand how major CHO cell manufacturing platforms diverge. We used matrix-assisted laser desorption ionization-time of flight mass spectrometry to perform N-glycomic analyses comparing CHO-K1 cells, CHO-S cells and antibody-producing daughter cell lines. The results reveal that genetic divergence in these industrially relevant cell lines, as well as the burden of antibody production, lead to significant differences in antennal branching and terminal elaboration in the cellular N-glycome. More specifically, CHO-K1 cells produce larger and more complex N-glycans with higher levels of sialylation than CHO-S cells, and antibody production was associated with increased antennal branching. Additionally, these findings were also reflected in the N-glycomic profiles of IgG1-Fc constructs produced in either CHO-K1 and CHO-S cells.

Indexed as

Genetic VariationPolysaccharidesAnimalsCHO CellsCricetinaeCricetulusGlycomicsGlycosylationRecombinant ProteinsPolysaccharidesRecombinant Proteinsantibody glycoengineeringbiopharmaceuticalsChinese hamster ovary (CHO) cellsMALDI‐TOFmass spectrometryN‐glycosylation

Identifiers

PMID40817708
PMCPMC12503014

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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.