Author: Shuai Xia; Meiqin Liu; Chao Wang; Wei Xu; Qiaoshuai Lan; Siliang Feng; Feifei Qi; Linlin Bao; Lanying Du; Shuwen Liu; Chuan Qin; Fei Sun; Zhengli Shi; Yun Zhu; Shibo Jiang; Lu Lu
Title: Inhibition of SARS-CoV-2 infection (previously 2019-nCoV) by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion Document date: 2020_3_12
ID: j5bepvvw_2
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.09.983247 doi: bioRxiv preprint S2 subunit plays a very important role in the membrane fusion process mediated by 167 MERS-CoV or SARS-CoV S protein 16, 17 . Similarly, our recent study suggested that 168 HR1 and HR2 in subunit S2 of SARS-CoV-2 also interacted to form coiled-coil 169 complex to support membrane fusion and viral infection .....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.09.983247 doi: bioRxiv preprint S2 subunit plays a very important role in the membrane fusion process mediated by 167 MERS-CoV or SARS-CoV S protein 16, 17 . Similarly, our recent study suggested that 168 HR1 and HR2 in subunit S2 of SARS-CoV-2 also interacted to form coiled-coil 169 complex to support membrane fusion and viral infection 15 ( Fig. 2a and Fig. S2 ).
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