Characterization of the SARS-CoV-2 Spike in an Early Prefusion Conformation

Tingting Li; Qingbing Zheng; Hai Yu; Dinghui Wu; Wenhui Xue; Yuyun Zhang; Xiaofen Huang; Lizhi Zhou; Zhigang Zhang; Zhenghui Zha; Tingting Chen; Zhiping Wang; Jie Chen; Hui Sun; Tingting Deng; Yingbin Wang; Yixin Chen; Qinjian Zhao; Jun Zhang; Ying Gu; Shaowei Li; Ningshao Xia

On the other hand, we investigated the glycosylation extent of the three protein by The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.16.994152 doi: bioRxiv preprint Reactivity of SARS-CoV-2 RBD, S1 and S proteins against convalescent COVID-173 19 human sera 174 We next evaluated the antigenicity of the three versions of S proteins by WB and ELISA 175 using a panel of six COVID-19 convalescent human sera, which was collected from Taken together, RBD, S1 and S proteins from insect cells maintain the native-like The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.16.994152 doi: bioRxiv preprint phase of SARS-CoV-2 infection. Among these epitopes, most RBD epitopes are strictly 194 tertiary conformation-dependent sites that are damaged upon the mild denatured 195 condition of reductant and SDS treatment, NTD within S1 bears some linear epitopes, 196 whereas S2 part essentially has linear epitopes that are immunogenic in all COVID-19 197 patients (n=6). The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.16.994152 doi: bioRxiv preprint worthy noted that the compared prefusion SARS-CoV-2 S trimer was engineered with 216 site-directed mutations to stabilize prefusion conformation and expressed in 239F cells.