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7SBV

Structure of OC43 spike in complex with polyclonal Fab4 (Donor 269)

Summary for 7SBV
Entry DOI10.2210/pdb7sbv/pdb
EMDB information24989
DescriptorSpike protein, Human polyclonal Fab model with polyalanine backbone - Heavy chain, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordshcov, spike, oc43, polyclonal antibody, empem, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceHuman coronavirus OC43 (HCoV-OC43)
More
Total number of polymer chains5
Total formula weight485943.60
Authors
Bangaru, S.,Antanasijevic, A.,Ward, A. (deposition date: 2021-09-26, release date: 2022-05-04, Last modification date: 2024-10-23)
Primary citationBangaru, S.,Antanasijevic, A.,Kose, N.,Sewall, L.M.,Jackson, A.M.,Suryadevara, N.,Zhan, X.,Torres, J.L.,Copps, J.,de la Pena, A.T.,Crowe Jr., J.E.,Ward, A.B.
Structural mapping of antibody landscapes to human betacoronavirus spike proteins.
Sci Adv, 8:eabn2911-eabn2911, 2022
Cited by
PubMed Abstract: Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV-2) infections. We used electron microscopy-based polyclonal epitope mapping (EMPEM) to characterize the antibody specificities against β-CoV spike proteins in prepandemic (PP) sera or SARS-CoV-2 convalescent (SC) sera. We observed that most PP sera had antibodies specific to seasonal human CoVs (HCoVs) OC43 and HKU1 spike proteins while the SC sera showed reactivity across all human β-CoVs. Detailed molecular mapping of spike-antibody complexes revealed epitopes that were differentially targeted by preexisting antibodies and SC serum antibodies. Our studies provide an antigenic landscape to β-HCoV spikes in the general population serving as a basis for cross-reactive epitope analyses in SARS-CoV-2-infected individuals.
PubMed: 35507649
DOI: 10.1126/sciadv.abn2911
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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