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. 2019 Apr 17;10:1799. doi: 10.1038/s41467-019-09608-w

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© This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Recombinant bacterial FTs and STs for live cell-surface glycan modification. a Specific positions on mammalian cell-surface LacNAc(Galβ1-4-GlcNAc)-containing glycans that can potentially be modified by fucosylation (α1-2- or α1-3-linked) and sialylation (α2-3- or α2-6-linked). Recombinant bacterial glycosyltransferases (FTs and STs) used in this study include Hm1,2FT, Hp1,3FT, Pm2,3ST-M144D, and Pd2,6ST. b Analysis of in vitro sialylation products by TLC. ++ indicates the final reaction system was further mixed with starting material LacNAc, and analyzed by TLC. c Analysis of in vitro fucosylation products by TLC. d, e Analysis of in vitro products generated by a combination of sialylation and fucosylation by TLC. sLe^X was formed by combining Hp1,3FT and Pm2,3ST-M144D (d). NeuAcα2-6-(Fucα1-2)-LacNAc was formed by combining Hm1,2FT and Pm2,3ST-M144D (e). f, g Analysis of newly formed glycan epitopes on the cell-surface of Lec2 CHO cells via chemoenzymatic glycan modification. Modified cells were stained by lectins and analyzed by flow cytometry. h, i Evaluation of the substrate tolerance of bacterial sialyltransferases. Unnatural sugar CMP-SiaNAz bearing the azide group were tested for STs. In figures f–i, error bars represent the standard deviation of three biological replicates. ** indicated Welch’s t-test P < 0.01. Source data for figures b–i are provided as a Source Data file