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8QTD

Local refinement of SARS-CoV-2 BA.2.86 Spike and XBB-7 Fab

Summary for 8QTD
Entry DOI10.2210/pdb8qtd/pdb
EMDB information18649
DescriptorSpike glycoprotein,Fibritin, XBB-7 fab heavy chain, XBB-7 fab light chain (3 entities in total)
Functional Keywordsviral protein/immune system, sars-cov-2, xbb-7, rbd, spike, ba.2.86, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains3
Total formula weight167387.44
Authors
Ren, J.,Duyvesteyn, H.M.E.,Stuart, D.I. (deposition date: 2023-10-12, release date: 2024-05-08, Last modification date: 2024-11-06)
Primary citationLiu, 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: 38723626
DOI: 10.1016/j.xcrm.2024.101553
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

227111

數據於2024-11-06公開中

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