ArticleBioorganic chemistry2022
Site-selective sulfation of N-glycans by human GlcNAc-6-O-sulfotransferase 1 (CHST2) and chemoenzymatic synthesis of sulfated antibody glycoforms.
Article in Bioorganic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Chemoenzymatic synthesis of unusual antibody glycoforms using E. coli expressed human and bovine β-1,4-galactosyltransferase and their mutants.Carbohydrate research · 2026Article
- Defining substrate specificities ofOrganic chemistry frontiers : an international journal of organic chemistry · 2026Article
- Selective fluorination of Fc glycans enhances antibody-mediated effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- Upregulation of Sulfated N-Glycans in Serum as Predictive Biomarkers for Early-Stage Breast Cancer.International journal of molecular sciences · 2025Article
- Raider of the lostFrontiers in molecular biosciences · 2025Article
- Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands.Journal of the American Chemical Society · 2024Article
- Chemoenzymatic Synthesis of SulfatedJACS Au · 2024Article
- Phosphates as Assisting Groups in Glycan Synthesis.ACS central science · 2024Article
- Exploiting Substrate Specificities of 6-JACS Au · 2023Article
- Milk glycan metabolism by intestinal bifidobacteria: insights from comparative genomics.Critical reviews in biochemistry and molecular biologyReview
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Sulfation is a common modification of glycans and glycoproteins. Sulfated N-glycans have been identified in various glycoproteins and implicated for biological functions, but in vitro synthesis of structurally well-defined full length sulfated N-glycans remains to be described. We report here the first in vitro enzymatic sulfation of biantennary complex type N-glycans by recombinant human CHST2 (GlcNAc-6-O-sulfotransferase 1, GlcNAc6ST-1). We found that the sulfotransferase showed high antennary preference and could selectively sulfate the GlcNAc moiety located on the Manα1,3Man arm of the biantennary N-glycan. The glycan chain was further elongated by bacterial β1,4 galactosyltransferase from Neiserria meningitidis and human β1,4 galactosyltransferase IV（B4GALT4）, which led to the formation of different sulfated N-glycans. Using rituximab as a model IgG antibody, we further demonstrated that the sulfated N-glycans could be efficiently transferred to an intact antibody by using a chemoenzymatic Fc glycan remodeling method, providing homogeneous sulfated glycoforms of antibodies. Preliminary binding analysis indicated that sulfation did not affect the apparent affinity of the antibody for FcγIIIa receptor.
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