8F0H
Structure of SARS-CoV-2 spike with antibody Fabs 2A10 and 1H2 (Local refinement of the RBD and Fabs 1H2 and 2A10)
Summary for 8F0H
| Entry DOI | 10.2210/pdb8f0h/pdb |
| EMDB information | 28757 |
| Descriptor | Antibody Fab 1H2 heavy chain, Spike glycoprotein, Antibody Fab 1H2 light chain, ... (6 entities in total) |
| Functional Keywords | viral protein, glycoprotein, immune system, antibody, sars-cov-2, covid, viral protein-immune system complex, coronavirus, viral protein/immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 183886.92 |
| Authors | Yu, X.,Zyla, D.,Hastie, K.M.,Saphire, E.O. (deposition date: 2022-11-02, release date: 2023-05-03, Last modification date: 2024-11-20) |
| Primary citation | Hastie, K.M.,Yu, X.,Ana-Sosa-Batiz, F.,Zyla, D.S.,Harkins, S.S.,Hariharan, C.,Wasserman, H.,Zandonatti, M.A.,Miller, R.,Maule, E.,Kim, K.,Valentine, K.M.,Shresta, S.,Saphire, E.O. Potent Omicron-neutralizing antibodies isolated from a patient vaccinated 6 months before Omicron emergence. Cell Rep, 42:112421-112421, 2023 Cited by PubMed Abstract: Therapeutic antibodies are an important tool in the arsenal against coronavirus infection. However, most antibodies developed early in the pandemic have lost most or all efficacy against newly emergent strains of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), particularly those of the Omicron lineage. Here, we report the identification of a panel of vaccinee-derived antibodies that have broad-spectrum neutralization activity. Structural and biochemical characterization of the three broadest-spectrum antibodies reveal complementary footprints and differing requirements for avidity to overcome variant-associated mutations in their binding footprints. In the K18 mouse model of infection, these three antibodies exhibit protective efficacy against BA.1 and BA.2 infection. This study highlights the resilience and vulnerabilities of SARS-CoV-2 antibodies and provides road maps for further development of broad-spectrum therapeutics. PubMed: 37083327DOI: 10.1016/j.celrep.2023.112421 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.18 Å) |
Structure validation
Download full validation report
