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Chemoenzymatic modular assembly of O-GalNAc glycans for functional glycomics

Author

Listed:
  • Shuaishuai Wang

    (Georgia State University)

  • Congcong Chen

    (Georgia State University
    Shandong University
    National-Local Joint Engineering Laboratory of Polysaccharide Drugs)

  • 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
    Southern University of Science and Technology)

  • Peixue Ling

    (Shandong University
    National-Local Joint Engineering Laboratory of Polysaccharide Drugs
    Shandong University)

  • Wanyi Guan

    (Hebei Normal University)

  • Lei Li

    (Georgia State University)

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.

Suggested Citation

  • 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 & Lei Li, 2021. "Chemoenzymatic modular assembly of O-GalNAc glycans for functional glycomics," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23428-x
    DOI: 10.1038/s41467-021-23428-x
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    Cited by:

    1. Tomomi Sumida & Satoshi Hiraoka & Keiko Usui & Akihiro Ishiwata & Toru Sengoku & Keith A. Stubbs & Katsunori Tanaka & Shigeru Deguchi & Shinya Fushinobu & Takuro Nunoura, 2024. "Genetic and functional diversity of β-N-acetylgalactosamine-targeting glycosidases expanded by deep-sea metagenome analysis," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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