8CXP
Characterisation of a Seneca Valley Virus Thermostable Mutant
This is a non-PDB format compatible entry.
Summary for 8CXP
Entry DOI | 10.2210/pdb8cxp/pdb |
EMDB information | 27066 |
Descriptor | Capsid protein VP1, Capsid protein VP3, VP2, ... (4 entities in total) |
Functional Keywords | virus, picornavirus, svv, seneca valley virus, oncolytic virus |
Biological source | Senecavirus A More |
Total number of polymer chains | 4 |
Total formula weight | 94696.85 |
Authors | Jayawardena, N.,Bostina, M.,Strauss, M. (deposition date: 2022-05-22, release date: 2022-09-28, Last modification date: 2024-06-12) |
Primary citation | Jayawardena, N.,McCarthy, C.,Wang, I.,Waqqar, S.,Burga, L.N.,Strauss, M.,Bostina, M. Characterisation of a Seneca Valley virus thermostable mutant. Virology, 575:74-82, 2022 Cited by PubMed Abstract: 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. PubMed: 36084546DOI: 10.1016/j.virol.2022.08.015 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.47 Å) |
Structure validation
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