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7YKJ

Omicron RBDs bound with P3E6 Fab (one up and one down)

Summary for 7YKJ
Entry DOI10.2210/pdb7ykj/pdb
EMDB information33892
DescriptorSpike glycoprotein, P3E6 heavy chain, P3E6 light chain (3 entities in total)
Functional Keywordscovid-19, p3e6, omicron, spike protein, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
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Total number of polymer chains4
Total formula weight292807.66
Authors
Tang, B.,Dang, S. (deposition date: 2022-07-22, release date: 2022-12-28, Last modification date: 2023-01-18)
Primary citationLuo, M.,Zhou, B.,Reddem, E.R.,Tang, B.,Chen, B.,Zhou, R.,Liu, H.,Liu, L.,Katsamba, P.S.,Au, K.K.,Man, H.O.,To, K.K.,Yuen, K.Y.,Shapiro, L.,Dang, S.,Ho, D.D.,Chen, Z.
Structural insights into broadly neutralizing antibodies elicited by hybrid immunity against SARS-CoV-2.
Emerg Microbes Infect, 12:2146538-2146538, 2023
Cited by
PubMed Abstract: Increasing spread by SARS-CoV-2 Omicron variants challenges existing vaccines and broadly reactive neutralizing antibodies (bNAbs) against COVID-19. Here we determine the diversity, potency, breadth and structural insights of bNAbs derived from memory B cells of BNT162b2-vaccinee after homogeneous Omicron BA.1 breakthrough infection. The infection activates diverse memory B cell clonotypes for generating potent class I/II and III bNAbs with new epitopes mapped to the receptor-binding domain (RBD). The top eight bNAbs neutralize wildtype and BA.1 potently but display divergent IgH/IgL sequences and neuralization profiles against other variants of concern (VOCs). Two of them (P2D9 and P3E6) belonging to class III NAbs display comparable potency against BA.4/BA.5, although structural analysis reveals distinct modes of action. P3E6 neutralizes all variants tested through a unique bivalent interaction with two RBDs. Our findings provide new insights into hybrid immunity on BNT162b2-induced diverse memory B cells in response to Omicron breakthrough infection for generating diverse bNAbs with distinct structural basis.
PubMed: 36354024
DOI: 10.1080/22221751.2022.2146538
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

227111

數據於2024-11-06公開中

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