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
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
Nepřihlášeným uživatelům se plný text nezobrazuje