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While glycosylation of GM-CSF reduces immunogenicity and enhances serum bioavailability, it can also diminish receptor binding and bioactivity. Based on transcriptomic analysis of human T lymphocytes reported previously, GM-CSF\u2013producing cells exhibit elevated expression of Alpha-1,6-Mannosylglycoprotein 6-Beta-N-Acetylglucosaminyltransferase (\n                  <jats:italic>MGAT5<\/jats:italic>\n                  ), which encodes N-acetylglucosaminyltransferase V, an enzyme involved in N-glycan branching. Given this role of MGAT5 in glycosylation, we produced GM-CSF variants using glycoengineered Chinese hamster ovary cells to generate diverse glycoforms and assessed their bioactivity. Testing their activity on TF-1 cell proliferation, we found that decreases in GM-CSF\n                  <jats:italic>N<\/jats:italic>\n                  -glycan branching significantly suppressed its activity. These findings underscore the importance of glycosylation in modulating the efficacy and safety of GM-CSF-based therapeutics, suggesting that precise glycoengineering may be key to optimizing GM-CSF performance in clinical applications.\n                <\/jats:p>","DOI":"10.64898\/2026.02.17.706267","type":"posted-content","created":{"date-parts":[[2026,2,19]],"date-time":"2026-02-19T04:55:11Z","timestamp":1771476911000},"source":"Crossref","is-referenced-by-count":0,"title":["The Role of Glycan Structures in Modulating GM-CSF Bioactivity: Insights from Glycoengineering"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-9108-4702","authenticated-orcid":false,"given":"Ece","family":"Cagdas","sequence":"first","affiliation":[{"name":"Department of Biotechnology and Biomedicine, Technical University of Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4673-4419","authenticated-orcid":false,"given":"Sarah 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