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8R80

SARS-CoV-2 Delta RBD in complex with XBB-9 Fab and an anti-Fab nanobody

Summary for 8R80
Entry DOI10.2210/pdb8r80/pdb
Related8QRF 8QRG 8QSQ 8QTD
DescriptorXBB-9 Fab heavy chain, XBB-9 Fab light chain, Spike protein S1, ... (4 entities in total)
Functional Keywordssars-cov-2, rbd, ba.2.86, xbb.1.5, xbb.1.5.10, xbb.1.5.70, viral protein
Biological sourceHomo sapiens
More
Total number of polymer chains8
Total formula weight169573.34
Authors
Zhou, D.,Ren, J.,Stuart, D.I. (deposition date: 2023-11-27, release date: 2024-05-08, Last modification date: 2024-10-23)
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
X-RAY DIFFRACTION (4.03 Å)
Structure validation

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