A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein

M. Gordon Joyce; Rajeshwer S. Sankhala; Wei-Hung Chen; Misook Choe; Hongjun Bai; Agnes Hajduczki; Lianying Yan; Spencer L. Sterling; Caroline E. Peterson; Ethan C. Green; Clayton Smith; Natalia de Val; Mihret Amare; Paul Scott; Eric D. Laing; Christopher C. Broder; Morgane Rolland; Nelson L. Michael; Kayvon Modjarrad

The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.15.992883 doi: bioRxiv preprint author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.15.992883 doi: bioRxiv preprint Fig. S3 . Structural and sequence analysis of the CR3022 epitope. Analysis of the CR3022 footprint across betacoronaviruses. The CR3022 epitope on SARS-CoV-2 (China.Wuhan.30Dec19.402132) RBD is compared across betacoronaviruses. The epitope is numbered according to the Wuhan reference; the strength of the interaction between the Ab and the spike protein is indicated by the height and color of the histogram bars above the sequence alignment. Sequences are ordered based on their phylogenetic relationships based on a maximum likelihood phylogenetic tree derived from amino acid RBD sequences. The RBD structure is shown in surface representation and depicts mutations between SARS-CoV-1 and SARS-CoV-2 in red; the CR3022 epitope is outlined in white, with contact residues shown in stick representation. author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.15.992883 doi: bioRxiv preprint Fig. S4 . SARS-CoV-2 and SARS-CoV antibody epitope analysis. A Sequence alignment of SARS-CoV-2 and SARS-CoV RBD. Antibody and ACE2 receptor interacting residues are highlighted on the sequence. B Antibody epitopes and receptor binding sites are outlined on the surface of the SARS-CoV RBD structures. The Sequence differences between SARS-COV-2 and SARS-CoV are indicated by red coloring on the RBD surface. C Antibody epitopes are shown on the SARS-CoV RBD molecule depicted in ribbon representation. The CR3022 epitope is shown on the SARS-CoV-2 RBD molecule. author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10. 1101