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Plant-Produced Viral Nanoparticles as a Functionalized Catalytic Support for Metabolic Engineering

TitoloPlant-Produced Viral Nanoparticles as a Functionalized Catalytic Support for Metabolic Engineering
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2024
AutoriSator, Christian, Lico Chiara, Pannucci Elisa, Marchetti Luca, Baschieri Selene, Warzecha Heribert, and Santi L.
RivistaPlants
Volume13
Issue4
Paginazione503
Data di pubblicazioneJan-02-2024
ISSN22237747
Abstract

Substrate channeling could be very useful for plant metabolic engineering; hence, we propose that functionalized supramolecular self-assembly scaffolds can act as enzymatic hubs able to perform reactions in close contiguity. Virus nanoparticles (VNPs) offer an opportunity in this context, and we present a functionalization strategy to display different enzymes on the outer surface of three different VNPs produced in plants. Tomato bushy stunt virus (TBSV) and Potato virus X (PVX) plant viruses were functionalized by the genetic fusion of the E-coil peptide coding sequence to their respective coat proteins genes, while the enzyme lichenase was tagged with the K-coil peptide. Immobilized E-coil VNPs were able to interact in vitro with the plant-produced functionalized lichenase, and catalysis was demonstrated by employing a lichenase assay. To prove this concept in planta, the Hepatitis B core (HBc) virus-like particles (VLPs) were similarly functionalized by genetic fusion with the E-coil sequence, while acyl-activating enzyme 1, olivetolic acid synthase, and olivetolic acid cyclase enzymes were tagged with the K-coil. The transient co-expression of the K-coil-enzymes together with E-coil-VLPs allowed the establishment of the heterologous cannabinoid precursor biosynthetic pathway. Noteworthy, a significantly higher yield of olivetolic acid glucoside was achieved when the scaffold E-coil-VLPs were employed. © 2024 by the authors.

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URLhttps://www.mdpi.com/2223-7747/13/4/503
DOI10.3390/plants13040503
Titolo brevePlants
Citation Key12276