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<p>Although B7 family immune checkpoint molecules such as PD-L1/PD-1 have improved the treatment of cancer and autoimmune diseases, more such molecules are still needed to expand therapeutic options. This study focuses on a novel molecule, VSIG2—previous studies suggested that VSIG2 acts as a receptor involved in T cell development, but this study is the first to identify a different mechanism of action, confirming that VSIG2 can function as an immunosuppressive ligand present on the surface of activated antigen-presenting cells. It specifically binds to Nectin-2 and does not interact with well-known immune receptors like PD-1 or CTLA-4; this binding strongly inhibits T cell activation and proliferation. In experiments, the human VSIG2-Ig protein alleviated the symptoms of experimental autoimmune encephalomyelitis, while anti-VSIG2 antibodies inhibited the growth of pancreatic cancer. The interaction between VSIG2 and Nectin-2 can regulate the STAT1/IRF1/GBP2 signaling pathway in T cells, thereby modulating T cell responses, and this axis is expected to serve as a novel therapeutic target for autoimmune diseases and cancer.</p>

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VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月5日

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  • Xianbin Wang,
  • Rong Hu,
  • Kezhu Chen,
  • Keke He,
  • Yuandi Li,
  • Jie Gao,
  • Yishen Tian,
  • Guangshi Du,
  • Zuli Wang,
  • Youbo Zhao,
  • Laijun Lai,
  • Min Su

摘要

Although B7 family immune checkpoint molecules such as PD-L1/PD-1 have improved the treatment of cancer and autoimmune diseases, more such molecules are still needed to expand therapeutic options. This study focuses on a novel molecule, VSIG2—previous studies suggested that VSIG2 acts as a receptor involved in T cell development, but this study is the first to identify a different mechanism of action, confirming that VSIG2 can function as an immunosuppressive ligand present on the surface of activated antigen-presenting cells. It specifically binds to Nectin-2 and does not interact with well-known immune receptors like PD-1 or CTLA-4; this binding strongly inhibits T cell activation and proliferation. In experiments, the human VSIG2-Ig protein alleviated the symptoms of experimental autoimmune encephalomyelitis, while anti-VSIG2 antibodies inhibited the growth of pancreatic cancer. The interaction between VSIG2 and Nectin-2 can regulate the STAT1/IRF1/GBP2 signaling pathway in T cells, thereby modulating T cell responses, and this axis is expected to serve as a novel therapeutic target for autoimmune diseases and cancer.