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We recently demonstrated that tyrosine sulfation occurred on a bispecific antibody (bsAb) produced in Chinese hamster ovary (CHO) cells, using a multi\u2010enzymatic approach in combination with intact mass and peptide\u2010based mass spectrometry analysis supplemented with the use of synthetic peptides. Tyrosine sulfation needs to be controlled during the manufacturing process due to potential undesired effects, such as impact on potency and immunogenicity. Here, we report that tyrosine sulfation was not significantly inhibited by the addition of chemical inhibitors, such as sodium chlorate. Individual knockout and double knockout (DKO) of two key genes in the tyrosine sulfation pathway were carried out sequentially. Tyrosyl protein sulfotransferase 1\/2 (TPST1\/2) DKO by CRISPR\/Cas9 (clustered regularly interspaced short palindromic repeats\/CRISPR\u2010associated protein\u20109 nuclease)\u2010mediated gene editing eliminated tyrosine sulfation while maintaining cell growth, antibody production, and overall product quality.<\/jats:p>","DOI":"10.1002\/biot.70302","type":"journal-article","created":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T12:17:03Z","timestamp":1788351423000},"source":"Crossref","is-referenced-by-count":0,"title":["TPST Gene Knock\u2010Out Eliminates Tyrosine Sulfation on a Recombinant Antibody Produced in CHO Cells"],"prefix":"10.1002","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6659-3388","authenticated-orcid":false,"given":"Jacqualyn","family":"Schulman","sequence":"first","affiliation":[{"name":"Biologics Development Bristol Myers Squibb, Summit  New Jersey 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