Chemoenzymatic modular assembly of O-GalNAc glycans for functional glycomics

Shuaishuai Wang, Congcong Chen, Madhusudhan Reddy Gadi, Varma Saikam, Ding Liu, He Zhu, Roni Bollag, Kebin Liu, Xi Chen, Fengshan Wang, Peng George Wang (), Peixue Ling (), Wanyi Guan () and Lei Li ()
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Shuaishuai Wang: Georgia State University
Congcong Chen: Georgia State University
Madhusudhan Reddy Gadi: Georgia State University
Varma Saikam: Georgia State University
Ding Liu: Georgia State University
He Zhu: Georgia State University
Roni Bollag: Augusta University
Kebin Liu: Medical College of Georgia
Xi Chen: University of California
Fengshan Wang: Shandong University
Peng George Wang: Georgia State University
Peixue Ling: Shandong University
Wanyi Guan: Hebei Normal University
Lei Li: Georgia State University

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract O-GalNAc glycans (or mucin O-glycans) play pivotal roles in diverse biological and pathological processes, including tumor growth and progression. Structurally defined O-GalNAc glycans are essential for functional studies but synthetic challenges and their inherent structural diversity and complexity have limited access to these compounds. Herein, we report an efficient and robust chemoenzymatic modular assembly (CEMA) strategy to construct structurally diverse O-GalNAc glycans. The key to this strategy is the convergent assembly of O-GalNAc cores 1–4 and 6 from three chemical building blocks, followed by enzymatic diversification of the cores by 13 well-tailored enzyme modules. A total of 83 O-GalNAc glycans presenting various natural glycan epitopes are obtained and used to generate a unique synthetic mucin O-glycan microarray. Binding specificities of glycan-binding proteins (GBPs) including plant lectins and selected anti-glycan antibodies towards these O-GalNAc glycans are revealed by this microarray, promoting their applicability in functional O-glycomics. Serum samples from colorectal cancer patients and healthy controls are assayed using the array reveal higher bindings towards less common cores 3, 4, and 6 than abundant cores 1 and 2, providing insights into O-GalNAc glycan structure-activity relationships.

Date: 2021
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DOI: 10.1038/s41467-021-23428-x

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