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dc.contributor.author | Bekker, Shani![]() |
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dc.contributor.author | Huismans, H. (Henk), 1942-![]() |
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dc.contributor.author | Van Staden, Vida![]() |
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dc.date.accessioned | 2023-03-17T05:52:16Z | |
dc.date.available | 2023-03-17T05:52:16Z | |
dc.date.issued | 2022-07-26 | |
dc.description | SUPPLEMENTARY MATERIAL : FIGURE S1: Solubility assay of modified VP7 proteins; FIGURE S2: Intracellular distribution of VP7 mutant proteins via indirect immunofluorescence microscopy; VIDEO S1: (A) and (B): Colocalisation analysis of WT VP7 with VP3. | en_US |
dc.description.abstract | A unique characteristic of the African horse sickness virus (AHSV) major core protein VP7 is that it is highly insoluble, and spontaneously forms crystalline particles in AHSV-infected cells and when expressed in vitro. The aggregation of AHSV VP7 into these crystals presents many problems in AHSV vaccine development, and it is unclear whether VP7 aggregation affects AHSV assembly or contributes to AHSV pathogenesis. Here, we set out to abolish VP7 self-assembly by targeting candidate amino acid regions on the surface of the VP7 trimer via site-directed mutagenesis. It was found that the substitution of seven amino acids resulted in the complete disruption of AHSV VP7 self-assembly, which abolished the formation of VP7 crystalline particles and converted VP7 to a fully soluble protein still capable of interacting with VP3 to form core-like particles. This work provides further insight into the formation of AHSV VP7 crystalline particles and the successful development of AHSV vaccines. It also paves the way for future research by drawing comparisons with similar viral phenomena observed in human virology. | en_US |
dc.description.department | Biochemistry | en_US |
dc.description.department | Genetics | en_US |
dc.description.department | Microbiology and Plant Pathology | en_US |
dc.description.librarian | am2023 | en_US |
dc.description.sponsorship | The National Research Foundation, the Poliomyelitis Research Foundation and the University of Pretoria, South Africa. | en_US |
dc.description.uri | https://www.mdpi.com/journal/viruses | en_US |
dc.identifier.citation | Bekker, S.; Huismans, H.; van Staden, V. Generation of a Soluble African Horse Sickness Virus VP7 Protein Capable of Forming Core-like Particles. Viruses 2022, 14, 1624. https://DOI.org/10.3390/v14081624. | en_US |
dc.identifier.issn | 1999-4915 (online) | |
dc.identifier.other | 10.3390/v14081624 | |
dc.identifier.uri | http://hdl.handle.net/2263/90151 | |
dc.language.iso | en | en_US |
dc.publisher | MDPI | en_US |
dc.rights | © 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license. | en_US |
dc.subject | VP7 | en_US |
dc.subject | Mutagenesis | en_US |
dc.subject | Solubility | en_US |
dc.subject | Crystalline particle | en_US |
dc.subject | Core-like particle | en_US |
dc.subject | Virus-like particle | en_US |
dc.subject | Vaccine | en_US |
dc.subject | Equine | en_US |
dc.subject | African horse sickness virus (AHSV) | en_US |
dc.title | Generation of a soluble African horse sickness virus VP7 protein capable of forming core-like particles | en_US |
dc.type | Article | en_US |