Cargando…
Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles
Plant viruses can be genetically modified to generate chimeric virus particles (CVPs) carrying heterologous peptides fused on the surface of coat protein (CP) subunits as vaccine candidates. However, some factors may be especially significant in determining the properties of chimeras. In this study,...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8067224/ https://www.ncbi.nlm.nih.gov/pubmed/33805417 http://dx.doi.org/10.3390/v13040572 |
_version_ | 1783682753113358336 |
---|---|
author | Chen, Tsung-Hsien Hu, Chung-Chi Lee, Chin-Wei Feng, Yu-Min Lin, Na-Sheng Hsu, Yau-Heiu |
author_facet | Chen, Tsung-Hsien Hu, Chung-Chi Lee, Chin-Wei Feng, Yu-Min Lin, Na-Sheng Hsu, Yau-Heiu |
author_sort | Chen, Tsung-Hsien |
collection | PubMed |
description | Plant viruses can be genetically modified to generate chimeric virus particles (CVPs) carrying heterologous peptides fused on the surface of coat protein (CP) subunits as vaccine candidates. However, some factors may be especially significant in determining the properties of chimeras. In this study, peptides from various sources and of various lengths were inserted into the Bamboo mosaic virus-based (BaMV) vector CP N-terminus to examine the chimeras infecting and accumulating in plants. Interestingly, it was found that the two different strains Foot-and-mouth disease virus (FMDV) VP1 antigens with flexible linker peptides (77 or 82 amino acids) were directly expressed on the BaMV CP, and the chimeric particles self-assembled and continued to express FMDV antigens. The chimeric CP, when directly fused with a large foreign protein (117 amino acids), can self-fold into incomplete virus particles or disks. The physicochemical properties of heterologus peptides N-terminus, complex strand structures of heterologus peptides C-terminus and different flexible linker peptides, can affect the chimera accumulation. Based on these findings, using plant virus-based chimeras to express foreign proteins can increase their length limitations, and engineered plant-made CVP-based vaccines have increasing potential for further development as novel vaccines. |
format | Online Article Text |
id | pubmed-8067224 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80672242021-04-25 Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles Chen, Tsung-Hsien Hu, Chung-Chi Lee, Chin-Wei Feng, Yu-Min Lin, Na-Sheng Hsu, Yau-Heiu Viruses Article Plant viruses can be genetically modified to generate chimeric virus particles (CVPs) carrying heterologous peptides fused on the surface of coat protein (CP) subunits as vaccine candidates. However, some factors may be especially significant in determining the properties of chimeras. In this study, peptides from various sources and of various lengths were inserted into the Bamboo mosaic virus-based (BaMV) vector CP N-terminus to examine the chimeras infecting and accumulating in plants. Interestingly, it was found that the two different strains Foot-and-mouth disease virus (FMDV) VP1 antigens with flexible linker peptides (77 or 82 amino acids) were directly expressed on the BaMV CP, and the chimeric particles self-assembled and continued to express FMDV antigens. The chimeric CP, when directly fused with a large foreign protein (117 amino acids), can self-fold into incomplete virus particles or disks. The physicochemical properties of heterologus peptides N-terminus, complex strand structures of heterologus peptides C-terminus and different flexible linker peptides, can affect the chimera accumulation. Based on these findings, using plant virus-based chimeras to express foreign proteins can increase their length limitations, and engineered plant-made CVP-based vaccines have increasing potential for further development as novel vaccines. MDPI 2021-03-29 /pmc/articles/PMC8067224/ /pubmed/33805417 http://dx.doi.org/10.3390/v13040572 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Chen, Tsung-Hsien Hu, Chung-Chi Lee, Chin-Wei Feng, Yu-Min Lin, Na-Sheng Hsu, Yau-Heiu Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles |
title | Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles |
title_full | Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles |
title_fullStr | Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles |
title_full_unstemmed | Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles |
title_short | Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles |
title_sort | stable display of artificially long foreign antigens on chimeric bamboo mosaic virus particles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8067224/ https://www.ncbi.nlm.nih.gov/pubmed/33805417 http://dx.doi.org/10.3390/v13040572 |
work_keys_str_mv | AT chentsunghsien stabledisplayofartificiallylongforeignantigensonchimericbamboomosaicvirusparticles AT huchungchi stabledisplayofartificiallylongforeignantigensonchimericbamboomosaicvirusparticles AT leechinwei stabledisplayofartificiallylongforeignantigensonchimericbamboomosaicvirusparticles AT fengyumin stabledisplayofartificiallylongforeignantigensonchimericbamboomosaicvirusparticles AT linnasheng stabledisplayofartificiallylongforeignantigensonchimericbamboomosaicvirusparticles AT hsuyauheiu stabledisplayofartificiallylongforeignantigensonchimericbamboomosaicvirusparticles |