Chemoenzymatic synthesis of human natural killer-1-containing glycans and application as serum antibodies probes

Mehman Bunyatov, Margreet A. Wolfert, Lin Liu, Ruth Huizinga, Marco W.J. Schreurs, Bart C. Jacobs, Geert Jan Boons*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)

Abstract

Despite the versatility of enzyme-mediated oligosaccharide assembly, it has as a limitation that not all glycosyl transferases or glycan-modifying enzymes are readily available to install all natural occurring terminal epitopes. Here a chemoenzymatic strategy is described in which a core oligosaccharide is assembled enzymatically that is subjected to chemical manipulations to install complex terminal epitopes. It provided an unprecedented panel of human natural killer-1 (HSO3–3GlcAβ1–3Galβ1–4GlcNAc)-containing oligosaccharides and derivatives thereof. The compounds were printed as a microarray to examine binding specificities of serum antibodies of patients suffering from anti-myelin-associated glycoprotein neuropathy. All samples required glucuronic acid for antibody binding; however, variable dependence was observed for the length of the LacNAc chain and sulfation of glucuronic acid. Most serum samples required a lacto-neohexaose backbone indicating glycosphingolipids are being targeted. The clinical spectrum of immunoglobulin M monoclonal gammopathy varies, and the glycan microarray provides a more reliable platform for disease diagnosis and prognosis. [Figure not available: see fulltext.]

Original languageEnglish
Pages (from-to)85-98
Number of pages14
JournalNature Synthesis
Volume3
Issue number1
Early online date2 Oct 2023
DOIs
Publication statusPublished - Jan 2024

Bibliographical note

Publisher Copyright:
© 2023, The Author(s), under exclusive licence to Springer Nature Limited.

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