View source for 8hee


==Pentamer of FMDV (A/TUR/14/98)==
<StructureSection load='8hee' size='340' side='right'caption='[[8hee]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hee]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HEE 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]] 3.2&#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=8hee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hee OCA], [https://pdbe.org/8hee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hee RCSB], [https://www.ebi.ac.uk/pdbsum/8hee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hee ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A7D5BJ70_9PICO A0A7D5BJ70_9PICO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Unlike most other picornaviruses, foot-and-mouth disease (FMD) intact virions (146S) dissociate easily into small pentameric subunits (12S). This causes a dramatically decreased immunogenicity by a mechanism that remains elusive. Here, we present the high-resolution structures of 12S (3.2 A) and its immune complex of a single-domain antibody (VHH) targeting the particle interior (3.2 A), as well as two 146S-specific VHHs complexed to distinct sites on the 146S capsid surface (3.6 A and 2.9 A). The antigenic landscape of 146S is depicted using 13 known FMD virus-antibody complexes. Comparison of the immunogenicity of 146S and 12S in pigs, focusing on the resulting antigenic sites and incorporating structural analysis, reveals that dissociation of 146S leads to structural alteration and destruction of multiple epitopes, resulting in significant differences in antibody profiles/lineages induced by 12S and 146S. Furthermore, 146S generates higher synergistic neutralizing antibody titers compared to 12S, whereas both particles induce similar total FMD virus specific antibody titers. This study can guide the structure-based rational design of novel multivalent and broad-spectrum recombinant vaccines for protection against FMD.

Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail.,Li H, Liu P, Dong H, Dekker A, Harmsen MM, Guo H, Wang X, Sun S Nat Commun. 2024 Oct 10;15(1):8774. doi: 10.1038/s41467-024-53027-5. PMID:39389971<ref>PMID:39389971</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hee" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Foot-and-mouth disease virus]]
[[Category: Large Structures]]
[[Category: Dong H]]
[[Category: Li HZ]]