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9CWQ

Local refinement of the SARS-CoV-2 BA.2.86 NTD

Summary for 9CWQ
Entry DOI10.2210/pdb9cwq/pdb
EMDB information45971
DescriptorBA.2.86 Spike protein NTD, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordssarbecoviruses, spike glycoprotein, structural genomic, inhibitor, viral protein, minibinder, structural genomics, seattle structural genomics center for infectious disease, ssgcid
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
Total number of polymer chains1
Total formula weight36423.85
Authors
Lee, J.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2024-07-30, release date: 2026-01-21)
Primary citationLee, J.,Case, J.B.,Park, Y.J.,Ravichandran, R.,Asarnow, D.,Tortorici, M.A.,Brown, J.T.,Sanapala, S.,Carter, L.,Baker, D.,Diamond, M.S.,Veesler, D.
The computationally designed TRI2-2 miniprotein inhibitor protects against multiple SARS-CoV-2 Omicron variants.
Commun Biol, 2026
Cited by
PubMed Abstract: The continued evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has compromised neutralizing antibody responses elicited by prior infection or vaccination and abolished the utility of most monoclonal antibody therapeutics. We previously described a computationally-designed, homotrimeric miniprotein inhibitor, designated TRI2-2, that protects mice against pre-Omicron SARS-CoV-2 variants. Here, we show that TRI2-2 exhibits broadly neutralizing activity of SARS-CoV-2 variants and protects mice against BQ.1.1, XBB.1.5 and BA.2.86 challenge when administered intranasally post-exposure. The resistance of TRI2-2 to viral escape by most variants and the ability to deliver it directly to the upper airways highlight the potential of the multivalent miniprotein inhibitor as an alternative therapeutic modality.
PubMed: 41519898
DOI: 10.1038/s42003-025-09499-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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PDB entries from 2026-01-14

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