View source for 9fwe


==N-VelcroVax HBcAg with SUMO-Affimer inserted at N-terminus (T=3 VLP)==
<StructureSection load='9fwe' size='340' side='right'caption='[[9fwe]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fwe]] is a 3 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=9FWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FWE 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]] 3.5&#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=9fwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fwe OCA], [https://pdbe.org/9fwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fwe RCSB], [https://www.ebi.ac.uk/pdbsum/9fwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fwe ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Nanoparticle presentation systems offer the potential to develop new vaccines rapidly in response to emerging diseases, a public health need that has become increasingly evident in the wake of the COVID-19 pandemic. Previously, we reported a nanoparticle scaffold system termed VelcroVax. This was constructed by insertion of a high affinity SUMO binding protein (Affimer), able to recognise a SUMO peptide tag, into the major immunodominant region of VLPs assembled from a tandem (fused dimer) form of hepatitis B virus (HBV) core protein (HBc). Here we describe an alternative form, termed N-VelcroVax, a VLP vaccine platform assembled from a monomeric HBc protein (N-anti-SUMO Affimer HBc 190) with the Affimer inserted at the N-terminus. In contrast to the tandem form of VelcroVax, N-VelcroVax VLPs were expressed well in E. coli. The VLPs effectively bound SUMO-tagged Junin virus glycoprotein, gp1 as assessed by structural and serological analyses. Cryo-EM characterisation of N-VelcroVax complexed with a SUMO-Junin gp1 showed continuous density attributable to the fused Affimer, in addition to evidence of target antigen capture. Collectively, these data suggest that N-VelcroVax has potential as a versatile next generation vaccine scaffold.

A VLP vaccine platform comprising the core protein of hepatitis B virus with N-terminal antigen capture.,Fatema K, Snowden JS, Watson A, Sherry L, Ranson NA, Stonehouse NJ, Rowlands DJ Int J Biol Macromol. 2025 Feb 15;305(Pt 2):141152. doi: , 10.1016/j.ijbiomac.2025.141152. PMID:39961558<ref>PMID:39961558</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 9fwe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Fatema K]]
[[Category: Ranson NA]]
[[Category: Rowlands DJ]]
[[Category: Sherry L]]
[[Category: Snowden JS]]
[[Category: Stonehouse NJ]]
[[Category: Watson A]]