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Huo, Jiandong; Le Bas, Audrey; Ruza, Reinis R; Duyvesteyn, Helen M E; Mikolajek, Halina; Malinauskas, Tomas; Tan, Tiong Kit; Rijal, Pramila; Dumoux, Maud; Ward, Philip N; Ren, Jingshan; Zhou, Daming; Harrison, Peter J; Weckener, Miriam; Clare, Daniel K; Vogirala, Vinod K; Radecke, Julika; Moynié, Lucile; Zhao, Yuguang; Gilbert-Jaramillo, Javier; Knight, Michael L; Tree, Julia A; Buttigieg, Karen R; Coombes, Naomi; Elmore, Michael J; Carroll, Miles W; Carrique, Loic; Shah, Pranav N M; James, William; Townsend, Alain R; Stuart, David I; Owens, Raymond J; Naismith, James H
Nature structural & molecular biology, 09/2020, Volume: 27, Issue: 9Journal Article
The SARS-CoV-2 virus is more transmissible than previous coronaviruses and causes a more serious illness than influenza. The SARS-CoV-2 receptor binding domain (RBD) of the spike protein binds to the human angiotensin-converting enzyme 2 (ACE2) receptor as a prelude to viral entry into the cell. Using a naive llama single-domain antibody library and PCR-based maturation, we have produced two closely related nanobodies, H11-D4 and H11-H4, that bind RBD (K of 39 and 12 nM, respectively) and block its interaction with ACE2. Single-particle cryo-EM revealed that both nanobodies bind to all three RBDs in the spike trimer. Crystal structures of each nanobody-RBD complex revealed how both nanobodies recognize the same epitope, which partly overlaps with the ACE2 binding surface, explaining the blocking of the RBD-ACE2 interaction. Nanobody-Fc fusions showed neutralizing activity against SARS-CoV-2 (4-6 nM for H11-H4, 18 nM for H11-D4) and additive neutralization with the SARS-CoV-1/2 antibody CR3022.
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