8CMA
SARS-CoV-2 Delta-RBD complexed with BA.4/5-35 Fab
Summary for 8CMA
| Entry DOI | 10.2210/pdb8cma/pdb |
| Related | 8CBD 8CBE 8CBF 8CII 8CIM 8CIN |
| Descriptor | BA.4/5-35 heavy chain, Spike protein S1, BA.4/5-35 light chain, ... (4 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, beta-49, omi-42, ba.4/5-35, viral protein/immune system, viral protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 70351.71 |
| Authors | Zhou, D.,Ren, J.,Stuart, D.I. (deposition date: 2023-02-18, release date: 2024-02-28, Last modification date: 2024-11-13) |
| 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 (3.29 Å) |
Structure validation
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