Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition

Aberrant glycosylation, especially sialylation, on cell surface is often associated with cancer progression and immunosuppression. Over-sialylation of stage-specific embryonic antigen-4 (SSEA-4) to generate disialylGb5 (DSGb5) was reported to trigger Siglec-7 recognition and suppress NK-mediated tar...

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Main Authors: Kuo-Shiang Liao, Yixuan Zhou, Cinya Chung, Chih-Chuan Kung, Chien-Tai Ren, Chung-Yi Wu, Yi-Wei Lou, Po-Kai Chuang, Balázs Imre, Yves S. Y. Hsieh, Chi-Huey Wong
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Language:English
Published: MDPI AG 2025-05-01
Series:Molecules
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Online Access:https://www.mdpi.com/1420-3049/30/11/2264
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author Kuo-Shiang Liao
Yixuan Zhou
Cinya Chung
Chih-Chuan Kung
Chien-Tai Ren
Chung-Yi Wu
Yi-Wei Lou
Po-Kai Chuang
Balázs Imre
Yves S. Y. Hsieh
Chi-Huey Wong
author_facet Kuo-Shiang Liao
Yixuan Zhou
Cinya Chung
Chih-Chuan Kung
Chien-Tai Ren
Chung-Yi Wu
Yi-Wei Lou
Po-Kai Chuang
Balázs Imre
Yves S. Y. Hsieh
Chi-Huey Wong
author_sort Kuo-Shiang Liao
collection DOAJ
description Aberrant glycosylation, especially sialylation, on cell surface is often associated with cancer progression and immunosuppression. Over-sialylation of stage-specific embryonic antigen-4 (SSEA-4) to generate disialylGb5 (DSGb5) was reported to trigger Siglec-7 recognition and suppress NK-mediated target killing. In this study, efficient chemo-enzymatic and programmable one-pot methods were explored for the synthesis of DSGb5 and related sialosides for assembly of glycan microarrays and evaluation of binding specificity toward Siglecs-7, 9, 10, and 15 associated with immune checkpoint inhibition. The result showed weak binding of DSGb5 to these Siglecs; however, a truncated glycolyl glycan was identified to bind Siglec-10 strongly with a dissociation constant of 50 nM and exhibited a significant inhibition of Siglec-10 interacting with breast cancer cells.
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spelling doaj-art-c40379fbf22c4ff4ba1d58e39d593d232025-08-20T02:33:02ZengMDPI AGMolecules1420-30492025-05-013011226410.3390/molecules30112264Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint InhibitionKuo-Shiang Liao0Yixuan Zhou1Cinya Chung2Chih-Chuan Kung3Chien-Tai Ren4Chung-Yi Wu5Yi-Wei Lou6Po-Kai Chuang7Balázs Imre8Yves S. Y. Hsieh9Chi-Huey Wong10Genomics Research Center, Academia Sinica, Taipei 115, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanDepartment of Chemistry, The Scripps Research Institute, San Diego, CA 92037, USASchool of Pharmacy, Taipei Medical University, Taipei 110, TaiwanSchool of Pharmacy, Taipei Medical University, Taipei 110, TaiwanGenomics Research Center, Academia Sinica, Taipei 115, TaiwanAberrant glycosylation, especially sialylation, on cell surface is often associated with cancer progression and immunosuppression. Over-sialylation of stage-specific embryonic antigen-4 (SSEA-4) to generate disialylGb5 (DSGb5) was reported to trigger Siglec-7 recognition and suppress NK-mediated target killing. In this study, efficient chemo-enzymatic and programmable one-pot methods were explored for the synthesis of DSGb5 and related sialosides for assembly of glycan microarrays and evaluation of binding specificity toward Siglecs-7, 9, 10, and 15 associated with immune checkpoint inhibition. The result showed weak binding of DSGb5 to these Siglecs; however, a truncated glycolyl glycan was identified to bind Siglec-10 strongly with a dissociation constant of 50 nM and exhibited a significant inhibition of Siglec-10 interacting with breast cancer cells.https://www.mdpi.com/1420-3049/30/11/2264sialyl SSEA-4programmablechemoenzymatic synthesisglycolyl sialic acidimmune checkpoint
spellingShingle Kuo-Shiang Liao
Yixuan Zhou
Cinya Chung
Chih-Chuan Kung
Chien-Tai Ren
Chung-Yi Wu
Yi-Wei Lou
Po-Kai Chuang
Balázs Imre
Yves S. Y. Hsieh
Chi-Huey Wong
Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition
Molecules
sialyl SSEA-4
programmable
chemoenzymatic synthesis
glycolyl sialic acid
immune checkpoint
title Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition
title_full Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition
title_fullStr Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition
title_full_unstemmed Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition
title_short Chemical and Enzymatic Synthesis of DisialylGb5 and Other Sialosides for Glycan Array Assembly and Evaluation of Siglec-Mediated Immune Checkpoint Inhibition
title_sort chemical and enzymatic synthesis of disialylgb5 and other sialosides for glycan array assembly and evaluation of siglec mediated immune checkpoint inhibition
topic sialyl SSEA-4
programmable
chemoenzymatic synthesis
glycolyl sialic acid
immune checkpoint
url https://www.mdpi.com/1420-3049/30/11/2264
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