8H6F
Cryo-EM structure of SARS-CoV-2 Spike protein in complex with A6 repebody
Summary for 8H6F
| Entry DOI | 10.2210/pdb8h6f/pdb |
| Related | 7YCO |
| EMDB information | 34501 34511 |
| Descriptor | Spike glycoprotein, Repebody (A6), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 6 |
| Total formula weight | 499328.80 |
| Authors | |
| Primary citation | Kim, D.G.,Kim, U.,Park, I.H.,Ryu, B.,Yoo, Y.,Cha, J.S.,Yoon, G.Y.,Kim, S.H.,Oh, H.,Seo, J.Y.,Nam, K.T.,Seong, J.K.,Shin, J.S.,Cho, H.S.,Kim, H.S. A bivalent form of a RBD-specific synthetic antibody effectively neutralizes SARS-CoV-2 variants. Antiviral Res., 220:105738-105738, 2023 Cited by PubMed Abstract: Coronavirus Disease 2019 (COVID-19) pandemic is severely impacting the world, and tremendous efforts have been made to deal with it. Despite many advances in vaccines and therapeutics, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants remains an intractable challenge. We present a bivalent Receptor Binding Domain (RBD)-specific synthetic antibody, specific for the RBD of wild-type (lineage A), developed from a non-antibody protein scaffold composed of LRR (Leucine-rich repeat) modules through phage display. We further reinforced the unique feature of the synthetic antibody by constructing a tandem dimeric form. The resulting bivalent form showed a broader neutralizing activity against the variants. The in vivo neutralizing efficacy of the bivalent synthetic antibody was confirmed using a human ACE2-expressing mouse model that significantly alleviated viral titer and lung infection. The present approach can be used to develop a synthetic antibody showing a broader neutralizing activity against a multitude of SARS-CoV-2 variants. PubMed: 37944822DOI: 10.1016/j.antiviral.2023.105738 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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