Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system
Autor: | Yulia Meshcheriakova, George P. Lomonossoff, Hadrien Peyret, Jake Richardson, Daniel Ponndorf |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
Molecular biology viruses Green Fluorescent Proteins HIV Core Protein p24 Nicotiana benthamiana lcsh:Medicine Molecular engineering in plants 02 engineering and technology Protein Engineering complex mixtures Article law.invention Green fluorescent protein 03 medical and health sciences Antigen In vivo law Tobacco Vaccines Virus-Like Particle lcsh:Science Multidisciplinary biology Chemistry Molecular engineering fungi lcsh:R Proteins food and beverages virus diseases Nanobiotechnology 021001 nanoscience & nanotechnology biology.organism_classification Plants Genetically Modified Hepatitis B Core Antigens Recombinant Proteins Cell biology Plant Leaves Cytosol 030104 developmental biology Capsid Covalent bond Recombinant DNA lcsh:Q 0210 nano-technology Peptides Biotechnology |
Zdroj: | Scientific Reports, Vol 10, Iss 1, Pp 1-13 (2020) Scientific Reports |
ISSN: | 2045-2322 |
DOI: | 10.1038/s41598-020-74105-w |
Popis: | Virus-like particles (VLPs) can be used as nano-carriers and antigen-display systems in vaccine development and therapeutic applications. Conjugation of peptides or whole proteins to VLPs can be achieved using different methods such as the SpyTag/SpyCatcher system. Here we investigate the conjugation of tandem Hepatitis B core (tHBcAg) VLPs and the model antigen GFP in vivo in Nicotiana benthamiana. We show that tHBcAg VLPs could be successfully conjugated with GFP in the cytosol and ER without altering VLP formation or GFP fluorescence. Conjugation in the cytosol was more efficient when SpyCatcher was displayed on tHBcAg VLPs instead of being fused to GFP. This effect was even more obvious in the ER, showing that it is optimal to display SpyCatcher on the tHBcAg VLPs and SpyTag on the binding partner. To test transferability of the GFP results to other antigens, we successfully conjugated tHBcAg VLPs to the HIV capsid protein P24 in the cytosol. This work presents an efficient strategy which can lead to time and cost saving post-translational, covalent conjugation of recombinant proteins in plants. |
Databáze: | OpenAIRE |
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