Selected article for: "previous study and protein fragment antigenicity"
Author: Pingping Zhang; Qi Gao; Tang Wang; Yuehua Ke; Fei Mo; Ruizhong Jia; Wanbing Liu; Lei Liu; Shangen Zheng; Yuzhen Liu; Luping Li; Yao Wang; Lei Xu; Kun Hao; Ruifu Yang; Shiyue Li; Changqing Lin; Yong Zhao
Title: Evaluation of recombinant nucleocapsid and spike proteins for serological diagnosis of novel coronavirus disease 2019 (COVID-19)
  • Document date: 2020_3_20
    • ID: 7atoko6c_4
    Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.17.20036954 doi: medRxiv preprint 5 spike protein (S protein), envelope protein (E), membrane protein (M), and 1 nucleocapsid protein (N protein). Among them, the N-protein is the most abundant, 2 relatively conservative protein in coronaviruses; thus, it is often used as a diagnostic 3 antigen [7] . Our previous study showed that the ant.....
    Document: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.17.20036954 doi: medRxiv preprint 5 spike protein (S protein), envelope protein (E), membrane protein (M), and 1 nucleocapsid protein (N protein). Among them, the N-protein is the most abundant, 2 relatively conservative protein in coronaviruses; thus, it is often used as a diagnostic 3 antigen [7] . Our previous study showed that the antigenicity of the COOH terminus is 4 higher than that of the NH 2 terminus in the SARS-CoV N protein, and that the former 5 N protein fragment may have the same antigenicity as that seen with the full-length N 6 protein [8] . In contrast, the S protein is the common target when designing vaccines 7 based on neutralizing antibodies. It contains a receptor binding domain (S-RBD) in 8 the S1 subunit, which mediates receptor binding and membrane fusion [9, 10]. 9

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