Selected article for: "complement activation and little effect"
Author: Ting Gao; Mingdong Hu; Xiaopeng Zhang; Hongzhen Li; Lin Zhu; Hainan Liu; Qincai Dong; Zhang Zhang; Zhongyi Wang; Yong Hu; Yangbo Fu; Yanwen Jin; Kaitong Li; Songtao Zhao; Yongjiu Xiao; Shuping Luo; Lufeng Li; Lingfang Zhao; Junli Liu; Huailong Zhao; Yue Liu; Weihong Yang; Jing Peng; Xiaoyu Chen; Ping Li; Yaoning Liu; Yonghong Xie; Jibo Song; Lu Zhang; Qingjun Ma; Xiuwu Bian; Wei Chen; Xuan Liu; Qing Mao; Cheng Cao
Title: Highly pathogenic coronavirus N protein aggravates lung injury by MASP-2-mediated complement over-activation
  • Document date: 2020_3_30
    • ID: dxs8ggyh_22
    Snippet: Here we show that SARS-CoV, MERS-CoV and SARS-CoV-2 share a common mechanism connecting the viral N proteins to binding and potentiation of an MBL, Ca 2+dependent auto-activation of MASP-2, leading to the uncontrolled activation of complement cascade, as characterized by the enhanced C4 cleavage and complement deposition ( Fig. 1 and 2) . 25 The binding of N protein to MASP-2 amplifies the effects of MASP-2-mediated lectin pathway activation. N p.....
    Document: Here we show that SARS-CoV, MERS-CoV and SARS-CoV-2 share a common mechanism connecting the viral N proteins to binding and potentiation of an MBL, Ca 2+dependent auto-activation of MASP-2, leading to the uncontrolled activation of complement cascade, as characterized by the enhanced C4 cleavage and complement deposition ( Fig. 1 and 2) . 25 The binding of N protein to MASP-2 amplifies the effects of MASP-2-mediated lectin pathway activation. N protein mutants either failed to interact with MASP-2 or failed to form an N dimer have little or no effect on MASP-2-mediated lectin pathway activation ( Fig. 1C and 1D) , suggesting that the effects of N protein are dependent on binding and dimerization.

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