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. 2020 Aug 11;11:4017. doi: 10.1038/s41467-020-17847-5

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© The Author(s) 2020

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. 4 — The data summarises the specificity of the GH16 O-glycanases described in this report. From left to right the glycans are TetraLacNAc, TriLacNAc, paraLacto-N-neohexaose, Lacto-N-neotetraose, Lacto-N-tetraose, Lacto-N-triose, Galβ1,3GalNAc β1,3Galβ1,4Glc tetrasaccharide Blood group A hexasaccharide, Blood group B hexasaccharide, Blood group H pentasaccharide, LacNAc, Blood group H tetrasaccharide II, 3-sialyllactose and P1 antigen. The linkages are β unless otherwise labelled and the bonds cleaved are indicated by the black arrows. Partial and trace activity are the estimation of greater than or less than 50% degradation, respectively, under the assay conditions used. A more detailed summary can be found in Supplementary Table 4. The predicted cellular locations of each enzyme is indicated on the far right of each row.