22PD
Cryo EM structure of SARS-COV-2 (BA.4) RBD in complex with THZ937 Fab (local refine)
Summary for 22PD
| Entry DOI | 10.2210/pdb22pd/pdb |
| EMDB information | 68583 |
| Descriptor | THZ937 fab heavy chain, THZ937 fab light chain, SARS-CoV-2 BA.4 spike RBD, ... (4 entities in total) |
| Functional Keywords | sars-cov-2;antibody;, viral protein/immune system, viral protein-immune system complex |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 49036.75 |
| Authors | |
| Primary citation | Zhang, Q.,Chen, P.,Guo, F.,Zhou, R.,Guo, R.,Ge, X.,Yang, Q.,Xie, X.,Xia, W.,Fan, J.,Yang, Z.,Xu, Y.,Huang, H.,Li, J.,Wang, H.,Liao, H.,Shi, X.,Liu, N.,Chen, Y.,Chen, Z.,Ma, J.,Wang, X.,Zhang, T.,Zhang, L. Twenty-year persistence of SARS-CoV-1 immune imprinting shapes antibody responses to SARS-CoV-2 infection. Immunity, 2026 Cited by PubMed Abstract: Antibody imprinting is well recognized, yet its long-term dynamics and epitope specificity remain poorly understood. Here, we studied individuals sequentially infected with SARS-CoV-1 (SARS-1) and SARS-CoV-2 (SARS-2) over two decades and found durable imprinting of antibody responses following SARS-2 BF.7 breakthrough infection. Approximately 60% of isolated monoclonal antibodies were SARS-1 imprinted and targeted conserved receptor-binding domain regions, whereas 37% overcame imprinting to recognize the SARS-2 receptor-binding motif overlapping the ACE2-binding site. Notably, some SARS-1-only antibodies retained germline-like features and neutralizing activity 20 years after infection. One exceptionally imprinted broadly neutralizing antibody, THZ937, protected hamsters against contact and airborne transmission of Omicron EG.5.1, demonstrating the functional relevance of durable imprinted antibodies. Together, these findings define the remarkable longevity and molecular basis of antibody imprinting and provide insights for pan-sarbecovirus vaccine design. PubMed: 42705227DOI: 10.1016/j.immuni.2026.08.009 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.95 Å) |
Structure validation
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