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_2
Snippet: The complement system functions as an immune surveillance system that rapidly responds to infection. Activation of the complement system resulted in pathogen elimination and acute or chronic inflammation. Nevertheless, dysregulated complement activation has been implicated in the development of acute lung diseases induced by highly pathogenic viruses (12, 25 13). The complement system can be activated via the classical pathway (CP), the lectin pa.....
Document: The complement system functions as an immune surveillance system that rapidly responds to infection. Activation of the complement system resulted in pathogen elimination and acute or chronic inflammation. Nevertheless, dysregulated complement activation has been implicated in the development of acute lung diseases induced by highly pathogenic viruses (12, 25 13). The complement system can be activated via the classical pathway (CP), the lectin pathway (LP), or the alternative pathway (AP) (14). In the LP, mannan-binding lectin (MBL) (or ficolins) binds to carbohydrate arrays of mannan and N-acetylglucosamine residues on the surfaces of the viruses or the surfaces of virus-infected cells, resulting in the activation of MBL-associated serine protease-2 (MASP-2), the only known MBL-associated protease that can directly initiate 30 the complement cascade (15, 16) . MBL binds to SARS-CoV-infected cells in a dose-dependent, calcium-dependent, and mannan-inhibitable manner in vitro, enhancing the deposition of complement C4 on SARS-CoV (17) . The N-linked glycosylation site N330 on the SARS-CoV spike (S) protein is critical for the specific interactions with MBL (18). Although higher levels of activated complement C3 and C4 fragments were found in SARS patients, indicating the 35 activation of complement pathways (19, 20) , the mechanism of SARS-CoV-induced complement activation is not well understood. It is also unknown whether a similar pathogenesis occurs in SARS-CoV-2 infection.
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