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It employs the recombinant bacterial sialic acid polymerases, NmC\u2010PST and NmB\u2010PST, in combination with cytidine 5\u2019\u2010monophosphate\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetylneuraminic acid (CMP\u2010Neu5Ac) derivatives that have a benzoyl ester at C\u20109 or thioethyl ether at the C\u20105 acetamide of Neu5Ac. It results in products that lack glycosyl accepting properties and hence prevent polymerization. A rationale for the blocking behavior of the C\u20105 modification is provided by molecular dynamics simulations. The benzoyl ester can be removed by mild basic hydrolysis, and the thioethyl ether by reductive desulfurization to give natural Neu5Ac than can be extended in the next cycle of enzymatic sialylation and unmasking. The resulting oligosialosides are attractive materials for the development of bacterial vaccines and as probes to investigate the roles of oligosialosides in human physiology.\n                  <\/jats:p>","DOI":"10.1002\/anie.4872790","type":"journal-article","created":{"date-parts":[[2026,7,13]],"date-time":"2026-07-13T08:19:02Z","timestamp":1783930742000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Chemoenzymatic Synthesis of Well\u2010Defined \u03b1(2,8)\u2010 and \u03b1(2,9)\u2010Linked Oligosialosides"],"prefix":"10.1002","volume":"65","author":[{"given":"Jelle A.","family":"Fok","sequence":"first","affiliation":[{"name":"Division of Chemical Biology and Drug Discovery Utrecht Institute for Pharmaceutical Sciences Utrecht University  Utrecht the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keshav","family":"Kishor","sequence":"additional","affiliation":[{"name":"Complex 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