8cxp: Difference between revisions

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'''Unreleased structure'''


The entry 8cxp is ON HOLD  until 2024-05-22
==Characterisation of a Seneca Valley Virus Thermostable Mutant==
<StructureSection load='8cxp' size='340' side='right'caption='[[8cxp]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cxp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Senecavirus_A Senecavirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CXP 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]] 2.47&#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=8cxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cxp OCA], [https://pdbe.org/8cxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cxp RCSB], [https://www.ebi.ac.uk/pdbsum/8cxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cxp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Seneca Valley virus (SVV) is a newly discovered picornavirus in the Senecavirus genus. SVV-001 strain has shown promise as an oncolytic virus against tumors with neuroendocrine features. There is a need to use a structure-based approach to develop virus-like particles capable to mimicking the architecture of naturally occurring empty capsids that can be used as vaccines or as carriers for targeted cancer treatment. However, these empty capsids are inherently less stable, and tedious to purify. This warrants investigation into factors which confer the SVV capsid stability and into combining this knowledge to recombinantly express stable SVV VLPs. In this study, we isolated a thermostable mutant of SVV by thermal selection assays and we characterized a single mutation located in a capsid protein. The cryo-EM map of this mutant showed conformational shifts that facilitated the formation of additional hydrogen bonds and aromatic interactions, which could serve as capsid stabilizing factors.


Authors:  
Characterisation of a Seneca Valley virus thermostable mutant.,Jayawardena N, McCarthy C, Wang I, Waqqar S, Burga LN, Strauss M, Bostina M Virology. 2022 Oct;575:74-82. doi: 10.1016/j.virol.2022.08.015. Epub 2022 Aug 30. PMID:36084546<ref>PMID:36084546</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8cxp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Senecavirus A]]
[[Category: Bostina M]]
[[Category: Jayawardena N]]
[[Category: Strauss M]]

Latest revision as of 08:18, 12 June 2024

Characterisation of a Seneca Valley Virus Thermostable MutantCharacterisation of a Seneca Valley Virus Thermostable Mutant

Structural highlights

8cxp is a 4 chain structure with sequence from Senecavirus A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.47Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Seneca Valley virus (SVV) is a newly discovered picornavirus in the Senecavirus genus. SVV-001 strain has shown promise as an oncolytic virus against tumors with neuroendocrine features. There is a need to use a structure-based approach to develop virus-like particles capable to mimicking the architecture of naturally occurring empty capsids that can be used as vaccines or as carriers for targeted cancer treatment. However, these empty capsids are inherently less stable, and tedious to purify. This warrants investigation into factors which confer the SVV capsid stability and into combining this knowledge to recombinantly express stable SVV VLPs. In this study, we isolated a thermostable mutant of SVV by thermal selection assays and we characterized a single mutation located in a capsid protein. The cryo-EM map of this mutant showed conformational shifts that facilitated the formation of additional hydrogen bonds and aromatic interactions, which could serve as capsid stabilizing factors.

Characterisation of a Seneca Valley virus thermostable mutant.,Jayawardena N, McCarthy C, Wang I, Waqqar S, Burga LN, Strauss M, Bostina M Virology. 2022 Oct;575:74-82. doi: 10.1016/j.virol.2022.08.015. Epub 2022 Aug 30. PMID:36084546[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Jayawardena N, McCarthy C, Wang I, Waqqar S, Burga LN, Strauss M, Bostina M. Characterisation of a Seneca Valley virus thermostable mutant. Virology. 2022 Oct;575:74-82. doi: 10.1016/j.virol.2022.08.015. Epub 2022 Aug 30. PMID:36084546 doi:http://dx.doi.org/10.1016/j.virol.2022.08.015

8cxp, resolution 2.47Å

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