7T3M
SARS-CoV-2 S (Spike Glycoprotein) D614G with Three (3) RBDs Up, Bound to Antibody 2-7 scFv, composite map
Summary for 7T3M
| Entry DOI | 10.2210/pdb7t3m/pdb |
| EMDB information | 25663 |
| Descriptor | Spike glycoprotein, Antibody 2-7 scFv, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | virus, coronavirus, sars cov-2, sars-cov-2, spike, 2-7, d614g, rbd, 3 rbds up, three rbds up, scfv, complex, phage display, viral protein, local refinement, focused refinement, viral protein-immune system complex, viral protein/immune system |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 6 |
| Total formula weight | 483949.28 |
| Authors | Byrne, P.O.,McLellan, J.S. (deposition date: 2021-12-08, release date: 2022-08-24, Last modification date: 2025-05-28) |
| Primary citation | Chang, M.R.,Tomasovic, L.,Kuzmina, N.A.,Ronk, A.J.,Byrne, P.O.,Johnson, R.,Storm, N.,Olmedillas, E.,Hou, Y.J.,Schafer, A.,Leist, S.R.,Tse, L.V.,Ke, H.,Coherd, C.,Nguyen, K.,Kamkaew, M.,Honko, A.,Zhu, Q.,Alter, G.,Saphire, E.O.,McLellan, J.S.,Griffiths, A.,Baric, R.S.,Bukreyev, A.,Marasco, W.A. IgG-like bispecific antibodies with potent and synergistic neutralization against circulating SARS-CoV-2 variants of concern. Nat Commun, 13:5814-5814, 2022 Cited by PubMed Abstract: Monoclonal antibodies are a promising approach to treat COVID-19, however the emergence of SARS-CoV-2 variants has challenged the efficacy and future of these therapies. Antibody cocktails are being employed to mitigate these challenges, but neutralization escape remains a major challenge and alternative strategies are needed. Here we present two anti-SARS-CoV-2 spike binding antibodies, one Class 1 and one Class 4, selected from our non-immune human single-chain variable fragment (scFv) phage library, that are engineered into four, fully-human IgG-like bispecific antibodies (BsAb). Prophylaxis of hACE2 mice and post-infection treatment of golden hamsters demonstrates the efficacy of the monospecific antibodies against the original Wuhan strain, while promising in vitro results with the BsAbs demonstrate enhanced binding and distinct synergistic effects on neutralizing activity against circulating variants of concern. In particular, one BsAb engineered in a tandem scFv-Fc configuration shows synergistic neutralization activity against several variants of concern including B.1.617.2. This work provides evidence that synergistic neutralization can be achieved using a BsAb scaffold, and serves as a foundation for the future development of broadly reactive BsAbs against emerging variants of concern. PubMed: 36192374DOI: 10.1038/s41467-022-33030-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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