8R8K
XBB-4 Fab in complex with SARS-CoV-2 BA.2.12.1 Spike Glycoprotein
Summary for 8R8K
| Entry DOI | 10.2210/pdb8r8k/pdb |
| Related | 8CIN 8QTD 8R1C 8R1D |
| EMDB information | 19002 |
| Descriptor | Spike glycoprotein,Fibritin, XBB-4 Fab Heavy chain, XBB-4 Fab Light chain (3 entities in total) |
| Functional Keywords | sars-cov-2, spike, glycoprotein, coronavirus, antibody, fab, xbb.1.5, therapeutic, complex, neutralising, rbd, receptor binding domain, convalescent sera, viral protein, immune system, xbb-4, ba.2.12.1, omicron variant, virus, ba.2.86 |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 3 |
| Total formula weight | 190670.66 |
| Authors | Duyvesteyn, H.M.E.,Ren, J.,Stuart, D.I. (deposition date: 2023-11-29, release date: 2024-05-08, Last modification date: 2024-11-13) |
| Primary citation | Liu, C.,Zhou, D.,Dijokaite-Guraliuc, A.,Supasa, P.,Duyvesteyn, H.M.E.,Ginn, H.M.,Selvaraj, M.,Mentzer, A.J.,Das, R.,de Silva, T.I.,Ritter, T.G.,Plowright, M.,Newman, T.A.H.,Stafford, L.,Kronsteiner, B.,Temperton, N.,Lui, Y.,Fellermeyer, M.,Goulder, P.,Klenerman, P.,Dunachie, S.J.,Barton, M.I.,Kutuzov, M.A.,Dushek, O.,Fry, E.E.,Mongkolsapaya, J.,Ren, J.,Stuart, D.I.,Screaton, G.R. A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity. Cell Rep Med, 5:101553-101553, 2024 Cited by PubMed Abstract: BA.2.86, a recently described sublineage of SARS-CoV-2 Omicron, contains many mutations in the spike gene. It appears to have originated from BA.2 and is distinct from the XBB variants responsible for many infections in 2023. The global spread and plethora of mutations in BA.2.86 has caused concern that it may possess greater immune-evasive potential, leading to a new wave of infection. Here, we examine the ability of BA.2.86 to evade the antibody response to infection using a panel of vaccinated or naturally infected sera and find that it shows marginally less immune evasion than XBB.1.5. We locate BA.2.86 in the antigenic landscape of recent variants and look at its ability to escape panels of potent monoclonal antibodies generated against contemporary SARS-CoV-2 infections. We demonstrate, and provide a structural explanation for, increased affinity of BA.2.86 to ACE2, which may increase transmissibility. PubMed: 38723626DOI: 10.1016/j.xcrm.2024.101553 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.41 Å) |
Structure validation
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