8xps: Difference between revisions
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==Structure of Nipah virus Bangladesh string G protein ectodomain monomer bound to single-domain antibody n425 at 3.22 Angstroms overall resolution== | |||
<StructureSection load='8xps' size='340' side='right'caption='[[8xps]], [[Resolution|resolution]] 3.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8xps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Henipavirus_nipahense Henipavirus nipahense] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XPS 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]] 3.22Å</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=MAN:ALPHA-D-MANNOSE'>MAN</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=8xps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xps OCA], [https://pdbe.org/8xps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xps RCSB], [https://www.ebi.ac.uk/pdbsum/8xps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xps ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nipah virus infection, one of the top priority diseases recognized by the World Health Organization, underscores the urgent need to develop effective countermeasures against potential epidemics and pandemics. Here, we identify a fully human single-domain antibody that targets a highly conserved cryptic epitope situated at the dimeric interface of the Nipah virus G protein (receptor binding protein, RBP), as elucidated through structures by high-resolution cryo-electron microscopy (cryo-EM). This unique binding mode disrupts the tetramerization of the G protein, consequently obstructing the activation of the F protein and inhibiting viral membrane fusion. Furthermore, our investigations reveal that this compact antibody displays enhanced permeability across the blood-brain barrier (BBB) and demonstrates superior efficacy in eliminating pseudovirus within the brain in a murine model of Nipah virus infection, particularly compared to the well-characterized antibody m102.4 in an IgG1 format. Consequently, this single-domain antibody holds promise as a therapeutic candidate to prevent Nipah virus infections and has potential implications for vaccine development. | |||
Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.,Wang Y, Sun Y, Shen Z, Wang C, Qian J, Mao Q, Wang Y, Song W, Kong Y, Zhan C, Chen Z, Dimitrov DS, Yang Z, Jiang S, Wu F, Lu L, Ying T, Sun L, Wu Y Nat Commun. 2024 Aug 12;15(1):6892. doi: 10.1038/s41467-024-51066-6. PMID:39134522<ref>PMID:39134522</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Chen | <div class="pdbe-citations 8xps" style="background-color:#fffaf0;"></div> | ||
[[Category: Mao | == References == | ||
[[Category: Sun | <references/> | ||
[[Category: Sun | __TOC__ | ||
</StructureSection> | |||
[[Category: Henipavirus nipahense]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen Z]] | |||
[[Category: Mao Q]] | |||
[[Category: Sun L]] | |||
[[Category: Sun Y]] | |||
Latest revision as of 07:54, 18 September 2024
Structure of Nipah virus Bangladesh string G protein ectodomain monomer bound to single-domain antibody n425 at 3.22 Angstroms overall resolutionStructure of Nipah virus Bangladesh string G protein ectodomain monomer bound to single-domain antibody n425 at 3.22 Angstroms overall resolution
Structural highlights
Publication Abstract from PubMedNipah virus infection, one of the top priority diseases recognized by the World Health Organization, underscores the urgent need to develop effective countermeasures against potential epidemics and pandemics. Here, we identify a fully human single-domain antibody that targets a highly conserved cryptic epitope situated at the dimeric interface of the Nipah virus G protein (receptor binding protein, RBP), as elucidated through structures by high-resolution cryo-electron microscopy (cryo-EM). This unique binding mode disrupts the tetramerization of the G protein, consequently obstructing the activation of the F protein and inhibiting viral membrane fusion. Furthermore, our investigations reveal that this compact antibody displays enhanced permeability across the blood-brain barrier (BBB) and demonstrates superior efficacy in eliminating pseudovirus within the brain in a murine model of Nipah virus infection, particularly compared to the well-characterized antibody m102.4 in an IgG1 format. Consequently, this single-domain antibody holds promise as a therapeutic candidate to prevent Nipah virus infections and has potential implications for vaccine development. Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.,Wang Y, Sun Y, Shen Z, Wang C, Qian J, Mao Q, Wang Y, Song W, Kong Y, Zhan C, Chen Z, Dimitrov DS, Yang Z, Jiang S, Wu F, Lu L, Ying T, Sun L, Wu Y Nat Commun. 2024 Aug 12;15(1):6892. doi: 10.1038/s41467-024-51066-6. PMID:39134522[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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