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==== | ==Structure of the SARS-CoV-2 S 6P trimer in complex with the neutralizing antibody Fab fragment, C1717== | ||
<StructureSection load='7uar' size='340' side='right'caption='[[7uar]]' scene=''> | <StructureSection load='7uar' size='340' side='right'caption='[[7uar]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7uar]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UAR FirstGlance]. <br> | ||
</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=7uar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uar OCA], [https://pdbe.org/7uar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uar RCSB], [https://www.ebi.ac.uk/pdbsum/7uar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uar ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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=7uar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uar OCA], [https://pdbe.org/7uar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uar RCSB], [https://www.ebi.ac.uk/pdbsum/7uar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uar ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SARS-CoV-2 infection or vaccination produces neutralizing antibody responses that contribute to better clinical outcomes. The receptor-binding domain (RBD) and the N-terminal domain (NTD) of the spike trimer (S) constitute the two major neutralizing targets for antibodies. Here, we use NTD-specific probes to capture anti-NTD memory B cells in a longitudinal cohort of infected individuals, some of whom were vaccinated. We found 6 complementation groups of neutralizing antibodies. 58% targeted epitopes outside the NTD supersite, 58% neutralized either Gamma or Omicron, and 14% were broad neutralizers that also neutralized Omicron. Structural characterization revealed that broadly active antibodies targeted three epitopes outside the NTD supersite including a class that recognized both the NTD and SD2 domain. Rapid recruitment of memory B cells producing these antibodies into the plasma cell compartment upon re-infection likely contributes to the relatively benign course of subsequent infections with SARS-CoV-2 variants, including Omicron. | |||
Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins.,Wang Z, Muecksch F, Cho A, Gaebler C, Hoffmann HH, Ramos V, Zong S, Cipolla M, Johnson B, Schmidt F, DaSilva J, Bednarski E, Ben Tanfous T, Raspe R, Yao K, Lee YE, Chen T, Turroja M, Milard KG, Dizon J, Kaczynska A, Gazumyan A, Oliveira TY, Rice CM, Caskey M, Bieniasz PD, Hatziioannou T, Barnes CO, Nussenzweig MC Immunity. 2022 Jun 14;55(6):998-1012.e8. doi: 10.1016/j.immuni.2022.04.003. Epub , 2022 Apr 7. PMID:35447092<ref>PMID:35447092</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7uar" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Severe acute respiratory syndrome coronavirus 2]] | ||
[[Category: Barnes CO]] | |||
Latest revision as of 12:38, 9 October 2024
Structure of the SARS-CoV-2 S 6P trimer in complex with the neutralizing antibody Fab fragment, C1717Structure of the SARS-CoV-2 S 6P trimer in complex with the neutralizing antibody Fab fragment, C1717
Structural highlights
Publication Abstract from PubMedSARS-CoV-2 infection or vaccination produces neutralizing antibody responses that contribute to better clinical outcomes. The receptor-binding domain (RBD) and the N-terminal domain (NTD) of the spike trimer (S) constitute the two major neutralizing targets for antibodies. Here, we use NTD-specific probes to capture anti-NTD memory B cells in a longitudinal cohort of infected individuals, some of whom were vaccinated. We found 6 complementation groups of neutralizing antibodies. 58% targeted epitopes outside the NTD supersite, 58% neutralized either Gamma or Omicron, and 14% were broad neutralizers that also neutralized Omicron. Structural characterization revealed that broadly active antibodies targeted three epitopes outside the NTD supersite including a class that recognized both the NTD and SD2 domain. Rapid recruitment of memory B cells producing these antibodies into the plasma cell compartment upon re-infection likely contributes to the relatively benign course of subsequent infections with SARS-CoV-2 variants, including Omicron. Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins.,Wang Z, Muecksch F, Cho A, Gaebler C, Hoffmann HH, Ramos V, Zong S, Cipolla M, Johnson B, Schmidt F, DaSilva J, Bednarski E, Ben Tanfous T, Raspe R, Yao K, Lee YE, Chen T, Turroja M, Milard KG, Dizon J, Kaczynska A, Gazumyan A, Oliveira TY, Rice CM, Caskey M, Bieniasz PD, Hatziioannou T, Barnes CO, Nussenzweig MC Immunity. 2022 Jun 14;55(6):998-1012.e8. doi: 10.1016/j.immuni.2022.04.003. Epub , 2022 Apr 7. PMID:35447092[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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