Spike protein binding prediction with neutralizing antibodies of SARS-CoV-2

Tamina Park; Sang-Yeop Lee; Seil Kim; Mi Jeong Kim; Hong Gi Kim; Sangmi Jun; Seung Il Kim; Bum Tae Kim; Edmond Changkyun Park; Daeui Park

The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.02.22.951178 doi: bioRxiv preprint structure of SARS-CoV-2 RBD protein at the X-ray crystal structure of known antibody-antigen complex from 202 SARS and MERS (Fig. 3) . The structures of five antibodies including m396, 80R, F26G19, S230, and CR3022 203 developing to prevent SARS-CoV were aligned on SARS-CoV-2 S-RBD successfully (Fig. 3A) . The six MERS-204 CoV antibodies such as MERS-27, CDC2-C2, m336, 4C2, D12, and MCA1 were also aligned on SARS-CoV-2 205 S-RBD (Fig. 3B) . Because the X-ray crystal structure of CR3022 was not revealed, the optimized structure was 206 predicted using antibody homology modeling by 1000 structures generated using Rosetta program. As a results, 207 two SARS-CoV antibodies including CR3022 (-13.91 dG score) and F26G19 (-15.98 dG score) and MERS-CoV 208 D12 (-14.01 dG score) antibody had higher binding score than other antibodies with SARS-CoV-2 S-RBD 209 region. However, various MERS-CoV antibodies did not match SARS-CoV-2 because MERS-CoV antibodies 210 were interacted with the outter regon of S-RBD which was located in major linear epitope region 211 (EDGDYYRKQL) (Fig. 2) .