期刊
CHEMICAL COMMUNICATIONS
卷 57, 期 50, 页码 6209-6212出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc01834e
关键词
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资金
- Ministry of Science and Technology [108-2113-M-001-008, 107-2113-M-001-031]
- Institute of Biological Chemistry, Academia Sinica
The study demonstrated the interaction between CGL and the TLR4/MD2 complex in a protein-TLR4 binding model, suggesting potential therapeutic targeting of TLR4. CGL was shown to significantly suppress immune responses induced by lipopolysaccharide.
Toll-like receptor 4 (TLR4) recognizes various protein ligands; however, the protein-TLR4 binding model is unclear. Here we demonstrate a Crenomytilus grayanus lectin (CGL)-TLR4/MD2 model to show that CGL interacts with a TLR4/myeloid differentiation factor 2 (MD2) complex independently of sugar-binding properties. CGL could suppress lipopolysaccharide-induced immune responses significantly, suggesting that TLR4 itself has potential as a therapeutic target.
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