6vo0: Difference between revisions
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==BG505 SOSIP.v5.2 in complex with rabbit Fab 43A2== | |||
<StructureSection load='6vo0' size='340' side='right'caption='[[6vo0]], [[Resolution|resolution]] 3.52Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6vo0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VO0 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]] 3.52Å</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=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=6vo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vo0 OCA], [https://pdbe.org/6vo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vo0 RCSB], [https://www.ebi.ac.uk/pdbsum/6vo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vo0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we isolated monoclonal antibodies from a rabbit that did not exhibit glycan hole-dependent autologous serum neutralization. The antibodies did not compete with a previously isolated glycan hole-specific antibody but did compete with N332 glycan supersite broadly neutralizing antibodies. A 3.5-A cryoEM structure of one of the antibodies in complex with the BG505 SOSIP.v5.2 trimer demonstrated that while the epitope recognized overlapped the N332 glycan supersite by contacting the GDIR motif at the base of V3, primary contacts were located in the variable V1 loop. These data suggest that strain-specific responses to V1 may interfere with broadly neutralizing responses to the N332 glycan supersite and vaccine immunogens may require engineering to minimize these off-target responses or steer them toward a more desirable pathway. | |||
HIV envelope trimer-elicited autologous neutralizing antibodies bind a region overlapping the N332 glycan supersite.,Nogal B, McCoy LE, van Gils MJ, Cottrell CA, Voss JE, Andrabi R, Pauthner M, Liang CH, Messmer T, Nedellec R, Shin M, Turner HL, Ozorowski G, Sanders RW, Burton DR, Ward AB Sci Adv. 2020 Jun 5;6(23):eaba0512. doi: 10.1126/sciadv.aba0512. eCollection 2020, Jun. PMID:32548265<ref>PMID:32548265</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6vo0" style="background-color:#fffaf0;"></div> | ||
[[Category: Cottrell | |||
[[Category: Nogal | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[Gp120 3D structures|Gp120 3D structures]] | |||
*[[Gp41 3D Structures|Gp41 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human immunodeficiency virus 1]] | |||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: Cottrell CA]] | |||
[[Category: Nogal B]] | |||
[[Category: Ward AB]] | |||
Latest revision as of 11:25, 17 October 2024
BG505 SOSIP.v5.2 in complex with rabbit Fab 43A2BG505 SOSIP.v5.2 in complex with rabbit Fab 43A2
Structural highlights
Publication Abstract from PubMedTo date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we isolated monoclonal antibodies from a rabbit that did not exhibit glycan hole-dependent autologous serum neutralization. The antibodies did not compete with a previously isolated glycan hole-specific antibody but did compete with N332 glycan supersite broadly neutralizing antibodies. A 3.5-A cryoEM structure of one of the antibodies in complex with the BG505 SOSIP.v5.2 trimer demonstrated that while the epitope recognized overlapped the N332 glycan supersite by contacting the GDIR motif at the base of V3, primary contacts were located in the variable V1 loop. These data suggest that strain-specific responses to V1 may interfere with broadly neutralizing responses to the N332 glycan supersite and vaccine immunogens may require engineering to minimize these off-target responses or steer them toward a more desirable pathway. HIV envelope trimer-elicited autologous neutralizing antibodies bind a region overlapping the N332 glycan supersite.,Nogal B, McCoy LE, van Gils MJ, Cottrell CA, Voss JE, Andrabi R, Pauthner M, Liang CH, Messmer T, Nedellec R, Shin M, Turner HL, Ozorowski G, Sanders RW, Burton DR, Ward AB Sci Adv. 2020 Jun 5;6(23):eaba0512. doi: 10.1126/sciadv.aba0512. eCollection 2020, Jun. PMID:32548265[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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