RT Journal Article
SR Electronic
T1 The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.04.10.036418
DO 10.1101/2020.04.10.036418
A1 Quinlan, Brian D.
A1 Mou, Huihui
A1 Zhang, Lizhou
A1 Guo, Yan
A1 He, Wenhui
A1 Ojha, Amrita
A1 Parcells, Mark S.
A1 Luo, Guangxiang
A1 Li, Wenhui
A1 Zhong, Guocai
A1 Choe, Hyeryun
A1 Farzan, Michael
YR 2020
UL http://biorxiv.org/content/early/2020/04/12/2020.04.10.036418.abstract
AB The SARS-coronavirus 2 (SARS-CoV-2) spike (S) protein mediates entry of SARS-CoV-2 into cells expressing the angiotensin-converting enzyme 2 (ACE2). The S protein engages ACE2 through its receptor-binding domain (RBD), an independently folded 197-amino acid fragment of the 1273-amino acid S-protein protomer. Antibodies to the RBD domain of SARS-CoV (SARS-CoV-1), a closely related coronavirus which emerged in 2002-2003, have been shown to potently neutralize SARS-CoV-1 S-protein-mediated entry, and the presence of anti-RBD antibodies correlates with neutralization in SARS-CoV-2 convalescent sera. Here we show that immunization with the SARS-CoV-2 RBD elicits a robust neutralizing antibody response in rodents, comparable to 100 µg/ml of ACE2-Ig, a potent SARS-CoV-2 entry inhibitor. Importantly, anti-sera from immunized animals did not mediate antibody-dependent enhancement (ADE) of S-protein-mediated entry under conditions in which Zika virus ADE was readily observed. These data suggest that an RBD-based vaccine for SARS-CoV-2 could be safe and effective.Competing Interest StatementThe authors have declared no competing interest.