7sb3: Difference between revisions
New page: '''Unreleased structure''' The entry 7sb3 is ON HOLD Authors: Ward, A., Bangaru, S., Antanasijevic, A. Description: Structure of OC43 spike in complex with polyclonal Fab1 (Donor 269) ... |
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==Structure of OC43 spike in complex with polyclonal Fab1 (Donor 269)== | |||
<StructureSection load='7sb3' size='340' side='right'caption='[[7sb3]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7sb3]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_coronavirus_OC43 Human coronavirus OC43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SB3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8Z9:(6Z)-hexadec-6-enoic+acid'>8Z9</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7sb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sb3 OCA], [https://pdbe.org/7sb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sb3 RCSB], [https://www.ebi.ac.uk/pdbsum/7sb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sb3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0B4N7I3_CVHOC A0A0B4N7I3_CVHOC] Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099] Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 beta-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 beta-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 beta-HCoV spikes in the general population serving as a basis for cross-reactive epitope analyses in SARS-CoV-2-infected individuals. | |||
Structural mapping of antibody landscapes to human betacoronavirus spike proteins.,Bangaru S, Antanasijevic A, Kose N, Sewall LM, Jackson AM, Suryadevara N, Zhan X, Torres JL, Copps J, de la Pena AT, Crowe JE Jr, Ward AB Sci Adv. 2022 May 6;8(18):eabn2911. doi: 10.1126/sciadv.abn2911. Epub 2022 May 4. PMID:35507649<ref>PMID:35507649</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Antanasijevic | <div class="pdbe-citations 7sb3" style="background-color:#fffaf0;"></div> | ||
[[Category: Bangaru | |||
[[Category: Ward | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[Spike protein 3D structures|Spike protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Human coronavirus OC43]] | |||
[[Category: Large Structures]] | |||
[[Category: Antanasijevic A]] | |||
[[Category: Bangaru S]] | |||
[[Category: Ward A]] | |||
Latest revision as of 14:29, 23 October 2024
Structure of OC43 spike in complex with polyclonal Fab1 (Donor 269)Structure of OC43 spike in complex with polyclonal Fab1 (Donor 269)
Structural highlights
FunctionA0A0B4N7I3_CVHOC Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099] Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Publication Abstract from PubMedPreexisting 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 beta-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 beta-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 beta-HCoV spikes in the general population serving as a basis for cross-reactive epitope analyses in SARS-CoV-2-infected individuals. Structural mapping of antibody landscapes to human betacoronavirus spike proteins.,Bangaru S, Antanasijevic A, Kose N, Sewall LM, Jackson AM, Suryadevara N, Zhan X, Torres JL, Copps J, de la Pena AT, Crowe JE Jr, Ward AB Sci Adv. 2022 May 6;8(18):eabn2911. doi: 10.1126/sciadv.abn2911. Epub 2022 May 4. PMID:35507649[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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