Engineered SARS-CoV-2 receptor binding domain improves immunogenicity in mice and elicits protective immunity in hamsters
Dalvie, N. C.; Rodriguez-Aponte, S. A.; Hartwell, B. L.; Tostanoski, L. H.; Biedermann, A. M.; Crowell, L. E.; Kaur, K.; Kumru, O.; Carter, L.; Yu, J.; Chang, A.; McMahan, K.; Courant, T.; Lebas, C.; Lemnios, A. A.; Rodrigues, K. A.; Silva, M.; Johnston, R. S.; Naranjo, C. A.; Tracey, M. K.; Brady, J. R.; Whittaker, C. A.; Yun, D.; Kar, S.; Porto, M.; Lok, M.; Andersen, H.; Lewis, M. G.; Love, K. R.; Camp, D. L.; Silverman, J. M.; Kleanthous, H.; Joshi, S. B.; Volkin, D. B.; Dubois, P. M.; Collin, N.; King, N. P.; Barouch, D. H.; Irvine, D. J.; Love, J. C.
Show abstract
Global containment of COVID-19 still requires accessible and affordable vaccines for low- and middle-income countries (LMICs).1 Recently approved vaccines provide needed interventions, albeit at prices that may limit their global access.2 Subunit vaccines based on recombinant proteins are suited for large-volume microbial manufacturing to yield billions of doses annually, minimizing their manufacturing costs.3 These types of vaccines are well-established, proven interventions with multiple safe and efficacious commercial examples.4-6 Many vaccine candidates of this type for SARS-CoV-2 rely on sequences containing the receptor-binding domain (RBD), which mediates viral entry to cells via ACE2.7,8 Here we report an engineered sequence variant of RBD that exhibits high-yield manufacturability, high-affinity binding to ACE2, and enhanced immunogenicity after a single dose in mice compared to the Wuhan-Hu-1 variant used in current vaccines. Antibodies raised against the engineered protein exhibited heterotypic binding to the RBD from two recently reported SARS-CoV-2 variants of concern (501Y.V1/V2). Presentation of the engineered RBD on a designed virus-like particle (VLP) also reduced weight loss in hamsters upon viral challenge.
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