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Cyclic diguanylate monophosphate directly binds to human siderocalin and inhibits its antibacterial activity

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  • Weihui Li

    (National Key Laboratory of Agricultural Microbiology, Center for Proteomics Research, College of Life Science and Technology, Huazhong Agricultural University)

  • Tao Cui

    (National Key Laboratory of Agricultural Microbiology, Center for Proteomics Research, College of Life Science and Technology, Huazhong Agricultural University)

  • Lihua Hu

    (National Key Laboratory of Agricultural Microbiology, Center for Proteomics Research, College of Life Science and Technology, Huazhong Agricultural University)

  • Ziqing Wang

    (National Key Laboratory of Agricultural Microbiology, Center for Proteomics Research, College of Life Science and Technology, Huazhong Agricultural University)

  • Zongqiang Li

    (National Key Laboratory of Agricultural Microbiology, Center for Proteomics Research, College of Life Science and Technology, Huazhong Agricultural University)

  • Zheng-Guo He

    (National Key Laboratory of Agricultural Microbiology, Center for Proteomics Research, College of Life Science and Technology, Huazhong Agricultural University)

Abstract

Cyclic diguanylate monophosphate (c-di-GMP) is a well-conserved second messenger in bacteria. During infection, the innate immune system can also sense c-di-GMP; however, whether bacterial pathogens utilize c-di-GMP as a weapon to fight against host defense for survival and possible mechanisms underlying this process remain poorly understood. Siderocalin (LCN2) is a key antibacterial component of the innate immune system and sequesters bacterial siderophores to prevent acquisition of iron. Here we show that c-di-GMP can directly target the human LCN2 protein to inhibit its antibacterial activity. We demonstrate that c-di-GMP specifically binds to LCN2. In addition, c-di-GMP can compete with bacterial ferric siderophores to bind LCN2. Furthermore, c-di-GMP can significantly reduce LCN2-mediated inhibition on the in vitro growth of Escherichia coli. Thus, LCN2 acts as a c-di-GMP receptor. Our findings provide insight into the mechanism by which bacteria utilize c-di-GMP to interfere with the innate immune system for survival.

Suggested Citation

  • Weihui Li & Tao Cui & Lihua Hu & Ziqing Wang & Zongqiang Li & Zheng-Guo He, 2015. "Cyclic diguanylate monophosphate directly binds to human siderocalin and inhibits its antibacterial activity," Nature Communications, Nature, vol. 6(1), pages 1-9, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9330
    DOI: 10.1038/ncomms9330
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    Cited by:

    1. Xiaocui Ling & Xiao Liu & Kun Wang & Minhao Guo & Yanzhe Ou & Danting Li & Yulin Xiang & Jiachen Zheng & Lihua Hu & Hongyun Zhang & Weihui Li, 2024. "Lsr2 acts as a cyclic di-GMP receptor that promotes keto-mycolic acid synthesis and biofilm formation in mycobacteria," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Shuyu Li & Qinmeng Liu & Chongyi Duan & Jialin Li & Hengxi Sun & Lei Xu & Qiao Yang & Yao Wang & Xihui Shen & Lei Zhang, 2023. "c-di-GMP inhibits the DNA binding activity of H-NS in Salmonella," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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