Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System
Virus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete....
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| Format: | Article |
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MDPI AG
2021-03-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/6/3098 |
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| author | Aleksander Strugała Jakub Jagielski Karol Kamel Grzegorz Nowaczyk Marcin Radom Marek Figlerowicz Anna Urbanowicz |
| author_facet | Aleksander Strugała Jakub Jagielski Karol Kamel Grzegorz Nowaczyk Marcin Radom Marek Figlerowicz Anna Urbanowicz |
| author_sort | Aleksander Strugała |
| collection | DOAJ |
| description | Virus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete. VLP formation is governed by two types of interactions: protein–cargo and protein–protein. These interactions can be modulated by the physicochemical properties of the surroundings. Here, we used brome mosaic virus (BMV) capsid protein produced in an <i>E. coli</i> expression system to study the impact of ionic strength, pH and encapsulated cargo on the assembly of VLPs and their features. We showed that empty VLP assembly strongly depends on pH whereas ionic strength of the buffer plays secondary but significant role. Comparison of VLPs containing tRNA and polystyrene sulfonic acid (PSS) revealed that the structured tRNA profoundly increases VLPs stability. We also designed and produced mutated BMV capsid proteins that formed VLPs showing altered diameters and stability compared to VLPs composed of unmodified proteins. We also observed that VLPs containing unstructured polyelectrolyte (PSS) adopt compact but not necessarily more stable structures. Thus, our methodology of VLP production allows for obtaining different VLP variants and their adjustment to the incorporated cargo. |
| first_indexed | 2024-03-10T13:07:51Z |
| format | Article |
| id | doaj.art-88122fd238e542618c4b304920a797b3 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T13:07:51Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-88122fd238e542618c4b304920a797b32023-11-21T10:58:17ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-03-01226309810.3390/ijms22063098Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial SystemAleksander Strugała0Jakub Jagielski1Karol Kamel2Grzegorz Nowaczyk3Marcin Radom4Marek Figlerowicz5Anna Urbanowicz6Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, PolandNanoBioMedical Centre, Adam Mickiewicz University, 61-614 Poznan, PolandInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, PolandNanoBioMedical Centre, Adam Mickiewicz University, 61-614 Poznan, PolandInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, PolandInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, PolandInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, PolandVirus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete. VLP formation is governed by two types of interactions: protein–cargo and protein–protein. These interactions can be modulated by the physicochemical properties of the surroundings. Here, we used brome mosaic virus (BMV) capsid protein produced in an <i>E. coli</i> expression system to study the impact of ionic strength, pH and encapsulated cargo on the assembly of VLPs and their features. We showed that empty VLP assembly strongly depends on pH whereas ionic strength of the buffer plays secondary but significant role. Comparison of VLPs containing tRNA and polystyrene sulfonic acid (PSS) revealed that the structured tRNA profoundly increases VLPs stability. We also designed and produced mutated BMV capsid proteins that formed VLPs showing altered diameters and stability compared to VLPs composed of unmodified proteins. We also observed that VLPs containing unstructured polyelectrolyte (PSS) adopt compact but not necessarily more stable structures. Thus, our methodology of VLP production allows for obtaining different VLP variants and their adjustment to the incorporated cargo.https://www.mdpi.com/1422-0067/22/6/3098virus-like particlesbrome mosaic viruscapsidself-assembly |
| spellingShingle | Aleksander Strugała Jakub Jagielski Karol Kamel Grzegorz Nowaczyk Marcin Radom Marek Figlerowicz Anna Urbanowicz Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System International Journal of Molecular Sciences virus-like particles brome mosaic virus capsid self-assembly |
| title | Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System |
| title_full | Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System |
| title_fullStr | Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System |
| title_full_unstemmed | Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System |
| title_short | Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System |
| title_sort | virus like particles produced using the brome mosaic virus recombinant capsid protein expressed in a bacterial system |
| topic | virus-like particles brome mosaic virus capsid self-assembly |
| url | https://www.mdpi.com/1422-0067/22/6/3098 |
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