9FJK
Omicron BA.1 Spike protein with neutralizing NTD specific mAb K501SP6
Summary for 9FJK
| Entry DOI | 10.2210/pdb9fjk/pdb |
| EMDB information | 50503 |
| Descriptor | Spike glycoprotein,Fibritin, K501SP6 Fv Heavy Chain, K501SP6 Fv Light Chain (3 entities in total) |
| Functional Keywords | neutralizing antibody, conserved epitope, covid-19, spike, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
| Total number of polymer chains | 5 |
| Total formula weight | 452833.31 |
| Authors | Bjoernsson, K.H.,Walker, M.R.,Raghavan, S.S.R.,Ward, A.B.,Barfod, L.K. (deposition date: 2024-05-31, release date: 2024-08-14, Last modification date: 2025-02-26) |
| Primary citation | Walker, M.R.,Underwood, A.,Bjornsson, K.H.,Raghavan, S.S.R.,Bassi, M.R.,Binderup, A.,Pham, L.V.,Ramirez, S.,Pinholt, M.,Dagil, R.,Knudsen, A.S.,Idorn, M.,Soegaard, M.,Wang, K.,Ward, A.B.,Salanti, A.,Bukh, J.,Barfod, L. Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages. Commun Biol, 7:1239-1239, 2024 Cited by PubMed Abstract: The continuous emergence of SARS-CoV-2 variants of concern has rendered many therapeutic monoclonal antibodies (mAbs) ineffective. To date, there are no clinically authorized therapeutic antibodies effective against the recently circulating Omicron sub-lineages BA.2.86 and JN.1. Here, we report the isolation of broad and potent neutralizing human mAbs (HuMabs) from a healthcare worker infected with SARS-CoV-2 early in the pandemic. These include a genetically unique HuMab, named K501SP6, which can neutralize different Omicron sub-lineages, including BQ.1, XBB.1, BA.2.86 and JN.1, by targeting a highly conserved epitope on the N terminal domain, as well as an RBD-specific HuMab (K501SP3) with high potency towards earlier circulating variants that was escaped by the more recent Omicron sub-lineages through spike F486 and E484 substitutions. Characterizing SARS-CoV-2 spike-specific HuMabs, including broadly reactive non-RBD-specific HuMabs, can give insight into the immune mechanisms involved in neutralization and immune evasion, which can be a valuable addition to already existing SARS-CoV-2 therapies. PubMed: 39354108DOI: 10.1038/s42003-024-06951-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.84 Å) |
Structure validation
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