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<p>Innate immune sensing by RIG-I-like receptors (RLRs) and the cGAS-STING pathway is tightly regulated by glycosylation. This review summarizes how distinct glycosylation modalities shape antiviral signaling at multiple levels. <i>N</i>-glycosylation in the ER-Golgi is essential for STING folding, stability, and signaling competence, whereas aberrant glycan states disrupt DNA sensing. In contrast, cytosolic <i>O</i>-GlcNAcylation dynamically modulates RLR-cGAS pathways by regulating MAVS aggregation, suppressing IRF3 and NF-κB activation, and interfering with cGAS-DNA binding. We further discuss crosstalk between glycosylation, ubiquitination, and phosphorylation, metabolic regulation of UDP-GlcNAc flux, and pathogen- or tumor-driven glycosylation reprogramming, highlighting glycosylation enzymes as potential immunomodulatory targets.</p>

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Glycosylation as a dynamic regulator of RLR and cGAS-STING innate immune signalling pathways

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月24日

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  • Jie Tong,
  • Wuchao Zhang,
  • Mengzhou Xue,
  • Chunfu Zheng

摘要

Innate immune sensing by RIG-I-like receptors (RLRs) and the cGAS-STING pathway is tightly regulated by glycosylation. This review summarizes how distinct glycosylation modalities shape antiviral signaling at multiple levels. N-glycosylation in the ER-Golgi is essential for STING folding, stability, and signaling competence, whereas aberrant glycan states disrupt DNA sensing. In contrast, cytosolic O-GlcNAcylation dynamically modulates RLR-cGAS pathways by regulating MAVS aggregation, suppressing IRF3 and NF-κB activation, and interfering with cGAS-DNA binding. We further discuss crosstalk between glycosylation, ubiquitination, and phosphorylation, metabolic regulation of UDP-GlcNAc flux, and pathogen- or tumor-driven glycosylation reprogramming, highlighting glycosylation enzymes as potential immunomodulatory targets.