8CBD
SARS-CoV-2 Delta-RBD complexed with BA.4/5-1 and EY6A Fabs
Summary for 8CBD
| Entry DOI | 10.2210/pdb8cbd/pdb |
| Descriptor | Spike protein S1, BA.4/5-1 heavy chain, BA.4/5-1 light chain, ... (6 entities in total) |
| Functional Keywords | sars-cov-2, ba.4 mab, ba.5 mab, rbd, ba.4/5-1, ba.4/5-2, ba.4/5-5, ey6a, viral protein/immune system, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 15 |
| Total formula weight | 352237.41 |
| Authors | Zhou, D.,Ren, J.,Stuart, D.I. (deposition date: 2023-01-25, release date: 2024-02-07, Last modification date: 2024-11-20) |
| Primary citation | Liu, C.,Das, R.,Dijokaite-Guraliuc, A.,Zhou, D.,Mentzer, A.J.,Supasa, P.,Selvaraj, M.,Duyvesteyn, H.M.E.,Ritter, T.G.,Temperton, N.,Klenerman, P.,Dunachie, S.J.,Paterson, N.G.,Williams, M.A.,Hall, D.R.,Fry, E.E.,Mongkolsapaya, J.,Ren, J.,Stuart, D.I.,Screaton, G.R. Emerging variants develop total escape from potent monoclonal antibodies induced by BA.4/5 infection. Nat Commun, 15:3284-3284, 2024 Cited by PubMed Abstract: The rapid evolution of SARS-CoV-2 is driven in part by a need to evade the antibody response in the face of high levels of immunity. Here, we isolate spike (S) binding monoclonal antibodies (mAbs) from vaccinees who suffered vaccine break-through infections with Omicron sub lineages BA.4 or BA.5. Twenty eight potent antibodies are isolated and characterised functionally, and in some cases structurally. Since the emergence of BA.4/5, SARS-CoV-2 has continued to accrue mutations in the S protein, to understand this we characterize neutralization of a large panel of variants and demonstrate a steady attrition of neutralization by the panel of BA.4/5 mAbs culminating in total loss of function with recent XBB.1.5.70 variants containing the so-called 'FLip' mutations at positions 455 and 456. Interestingly, activity of some mAbs is regained on the recently reported variant BA.2.86. PubMed: 38627386DOI: 10.1038/s41467-024-47393-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.52 Å) |
Structure validation
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