TY - JOUR T1 - The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement JF - bioRxiv DO - 10.1101/2020.04.10.036418 SP - 2020.04.10.036418 AU - Brian D. Quinlan AU - Huihui Mou AU - Lizhou Zhang AU - Yan Guo AU - Wenhui He AU - Amrita Ojha AU - Mark S. Parcells AU - Guangxiang Luo AU - Wenhui Li AU - Guocai Zhong AU - Hyeryun Choe AU - Michael Farzan Y1 - 2020/01/01 UR - http://biorxiv.org/content/early/2020/04/12/2020.04.10.036418.abstract N2 - 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. ER -