11HO
1332D4 Spike KP3.1.1 Complex
Summary for 11HO
| Entry DOI | 10.2210/pdb11ho/pdb |
| EMDB information | 75698 |
| Descriptor | 1332D4 Heavy Chain, 1332D4 Light Chain, SARS-CoV-2 KP3.1.1 variant, ... (5 entities in total) |
| Functional Keywords | fab, complex, sars-cov-2, viral protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 468533.46 |
| Authors | Kizziah, J.L.,Walter, M.R. (deposition date: 2026-02-24, release date: 2026-08-26, Last modification date: 2026-09-02) |
| Primary citation | Piepenbrink, M.S.,Ma, Y.,Panjwani, S.,Blake, A.R.,Bell, A.M.,Kizziah, J.L.,Mahmoud, S.H.,Ippolito, G.C.,Erdmann, N.B.,Goepfert, P.A.,Martinez-Sobrido, L.,Kobie, J.J.,Walter, M.R. Emergence of neutralizing RBD antibodies following Omicron infection with limited activity against ancestral SARS-CoV-2. Iscience, 29:117166-117166, 2026 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) evolution reduces the efficacy of prophylactic vaccines and monoclonal antibody (mAb) therapies. To evaluate potency and breadth, receptor binding domain (RBD)-targeting neutralizing mAbs were identified from patient B cells using an Omicron KP3.1.1 Spike (S) protein bait. MAbs exhibiting the greatest neutralization potency (1332D4 and 1332E5) and binding breadth (1324A10 and 1316C10) were evaluated in greater detail. Cryo-electron microscopy (Cryo-EM) studies revealed 1332D4 and 1332E5 target RBD residue segments 439-446 and 498-506 of KP3.1.1 S, respectively. 1332E5 is a knob-targeting class-1/4 mAb that exhibits pan-Omicron specificity but does not bind or neutralize ancestral Wuhan-1. Further analysis suggests mAbs generically defined as class 1/4 mAbs may be separated into two classes. Class 1/4 mAbs, like 1332E5, and class 4/1 mAbs that make extensive interactions with the class-4 epitope and limited contacts with the class-1 knob. Despite these differences, the specificity of both mAb classes can be altered by mutations in knob. PubMed: 42621159DOI: 10.1016/j.isci.2026.117166 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.26 Å) |
Structure validation
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