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Glycosylation can influence the efficacy, serum half\u2010life, 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\u2010assisted laser desorption ionization\u2010time of flight mass spectrometry to perform N\u2010glycomic analyses comparing CHO\u2010K1 cells, CHO\u2010S cells and antibody\u2010producing 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\u2010glycome. More specifically, CHO\u2010K1 cells produce larger and more complex N\u2010glycans with higher levels of sialylation than CHO\u2010S cells, and antibody production was associated with increased antennal branching. Additionally, these findings were also reflected in the N\u2010glycomic profiles of IgG1\u2010Fc constructs produced in either CHO\u2010K1 and CHO\u2010S cells.<\/jats:p>","DOI":"10.1002\/bit.70045","type":"journal-article","created":{"date-parts":[[2025,8,16]],"date-time":"2025-08-16T07:34:27Z","timestamp":1755329667000},"page":"3160-3175","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Genetic Divergence and Antibody Expression Influence the N\u2010Glycomes of CHO\u2010K1 and CHO\u2010S Cells"],"prefix":"10.1002","volume":"122","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5270-2854","authenticated-orcid":false,"given":"Roberto","family":"Donini","sequence":"first","affiliation":[{"name":"Department of Life Sciences Imperial College London London 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