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8C89

SARS-CoV-2 spike in complex with the 17T2 neutralizing antibody Fab fragment (local refinement of RBD and Fab)

Summary for 8C89
Entry DOI10.2210/pdb8c89/pdb
EMDB information16473
DescriptorSpike protein S2', 17T2 Fab heavy chain, 17T2 Fab light chain, ... (4 entities in total)
Functional Keywordscomplex sars-cov-2 spike s 17t2, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus
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Total number of polymer chains3
Total formula weight72664.48
Authors
Modrego, A.,Carlero, D.,Bueno-Carrasco, M.T.,Santiago, C.,Carolis, C.,Arranz, R.,Blanco, J.,Magri, G. (deposition date: 2023-01-19, release date: 2024-01-10, Last modification date: 2024-11-13)
Primary citationde Campos-Mata, L.,Trinite, B.,Modrego, A.,Tejedor Vaquero, S.,Pradenas, E.,Pons-Grifols, A.,Rodrigo Melero, N.,Carlero, D.,Marfil, S.,Santiago, C.,Raich-Regue, D.,Bueno-Carrasco, M.T.,Tarres-Freixas, F.,Abanco, F.,Urrea, V.,Izquierdo-Useros, N.,Riveira-Munoz, E.,Ballana, E.,Perez, M.,Vergara-Alert, J.,Segales, J.,Carolis, C.,Arranz, R.,Blanco, J.,Magri, G.
A monoclonal antibody targeting a large surface of the receptor binding motif shows pan-neutralizing SARS-CoV-2 activity.
Nat Commun, 15:1051-1051, 2024
Cited by
PubMed Abstract: Here we report the characterization of 17T2, a SARS-CoV-2 pan-neutralizing human monoclonal antibody isolated from a COVID-19 convalescent individual infected during the first pandemic wave. 17T2 is a class 1 VH1-58/κ3-20 antibody, derived from a receptor binding domain (RBD)-specific IgA memory B cell, with a broad neutralizing activity against former and new SARS-CoV-2 variants, including XBB.1.16 and BA.2.86 Omicron subvariants. Consistently, 17T2 demonstrates in vivo prophylactic and therapeutic activity against Omicron BA.1.1 infection in K18-hACE2 mice. Cryo-electron microscopy reconstruction shows that 17T2 binds the BA.1 spike with the RBD in "up" position and blocks the receptor binding motif, as other structurally similar antibodies do, including S2E12. Yet, unlike S2E12, 17T2 retains its neutralizing activity against all variants tested, probably due to a larger RBD contact area. These results highlight the impact of small structural antibody changes on neutralizing performance and identify 17T2 as a potential candidate for future clinical interventions.
PubMed: 38316751
DOI: 10.1038/s41467-024-45171-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.41 Å)
Structure validation

238895

건을2025-07-16부터공개중

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