View source for 7sge


==I53-50 nanoparticle core reconstructed from GPC-I53-50NP by focused refinement==
<StructureSection load='7sge' size='340' side='right'caption='[[7sge]], [[Resolution|resolution]] 3.67&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sge]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SGE 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]] 3.67&#8491;</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=7sge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sge OCA], [https://pdbe.org/7sge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sge RCSB], [https://www.ebi.ac.uk/pdbsum/7sge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sge ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The Lassa virus is endemic in parts of West Africa, and it causes hemorrhagic fever with high mortality. The development of a recombinant protein vaccine has been hampered by the instability of soluble Lassa virus glycoprotein complex (GPC) trimers, which disassemble into monomeric subunits after expression. Here, we use two-component protein nanoparticles consisting of trimeric and pentameric subunits to stabilize GPC in a trimeric conformation. These GPC nanoparticles present twenty prefusion GPC trimers on the surface of an icosahedral particle. Cryo-EM studies of GPC nanoparticles demonstrated a well-ordered structure and yielded a high-resolution structure of an unliganded GPC. These nanoparticles induced potent humoral immune responses in rabbits and protective immunity against the lethal Lassa virus challenge in guinea pigs. Additionally, we isolated a neutralizing antibody that mapped to the putative receptor-binding site, revealing a previously undefined site of vulnerability. Collectively, these findings offer potential approaches to vaccine and therapeutic design for the Lassa virus.

Lassa virus glycoprotein nanoparticles elicit neutralizing antibody responses and protection.,Brouwer PJM, Antanasijevic A, Ronk AJ, Muller-Krauter H, Watanabe Y, Claireaux M, Perrett HR, Bijl TPL, Grobben M, Umotoy JC, Schriek AI, Burger JA, Tejjani K, Lloyd NM, Steijaert TH, van Haaren MM, Sliepen K, de Taeye SW, van Gils MJ, Crispin M, Strecker T, Bukreyev A, Ward AB, Sanders RW Cell Host Microbe. 2022 Dec 14;30(12):1759-1772.e12. doi: , 10.1016/j.chom.2022.10.018. Epub 2022 Nov 17. PMID:36400021<ref>PMID:36400021</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7sge" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Antanasijevic A]]
[[Category: Brouwer PJM]]
[[Category: Ward AB]]