Health Canada authorized a new COVID-19 vaccine Thursday that it touted as the first greenlit shot to be developed by a Canadian company and the first to be made with plant-based technology.
Known as Covifenz, the vaccine was developed by Medicago, a biotechnology company based in Quebec City that uses a plant host to make virus-like particles (VLPs) which help the body’s immune system make antibodies.
- Plant-based virus-like particles (VLP) of SARS-CoV-2 spike protein (original strain)
- AS03 Adjuvant (manufactured by GlaxoSmithKline):
- polysorbate 80
- phosphate buffered saline
- potassium phosphate monobasic anhydrous
- sodium chloride
- sodium phosphate dibasic anhydrous
- water for injection
May contain trace amounts of polyethylene glycol, kanamycin and carbenicillin
Transient and stable expression of the firefly luciferase gene in plant cells and transgenic plants
The luciferase gene from the firefly, Photinus pyralis, was used as a reporter of gene expression by light production in transfected plant cells and transgenic plants. A complementary DNA clone of the firefly luciferase gene under the control of a plant virus promoter (cauliflower mosaic virus 35S RNA promoter) was introduced into plant protoplast cells (Daucus carota) by electroporation and into plants (Nicotiana tabacum) by use of the Agrobacterium tumefaciens tumor-inducing plasmid.
Extracts from electroporated cells (24 hours after the introduction of DNA) and from transgenic plants produce light when mixed with the substrates luciferin and adenosine triphosphate. Light produced by the action of luciferase was also detected in undisrupted leaves or cells in culture from transgenic plants incubated in luciferin and in whole transgenic plants “watered” with luciferin. Although light was detected in most organs in intact, transgenic plants (leaves, stems, and roots), the pattern of luminescence appeared to reflect both the organ-specific distribution of luciferase and the pathway for uptake of luciferin through the vasculature of the plant.
RNA delivery with a human virus-like particle (VLP)
Virus sequences incorporated throughout the human genome raise the tantalizing possibility that their natural functions could be harnessed to deliver therapeutic RNA. Retroelements account for about 8% of the human genome2. Although most endogenous retroviral genes have lost their functions, some continue to have roles in human physiology. Several retroelements have been reported to retain some of their ancient functionality, such as binding and transferring mRNA and forming capsids within the cell2.
To find candidate retroelement genes suitable for RNA delivery, Segel et al.1 surveyed conserved endogenous retroelements, focusing on homologs of structural retroviral Gag proteins that contain the core capsid domain. This domain protects the genome of both retrotransposons and retroviruses by forming VLPs, suggesting that proteins that contain it might be able to transfer other RNAs. The authors narrowed down their search to proteins that are conserved between human and mouse and have detectable RNA levels, because such proteins are more likely to have retained some functionality in mammalian cells. They screened their leading hits in bacteria and mammalian cells to determine whether they are secreted in extracellular vesicles as VLPs. The protein most highly enriched in the VLP fraction was mouse (Mus musculus) PEG10, which is also detected at appreciable levels in mouse serum. Moreover, the VLPs formed by the PEG10 protein contained the full-length Peg10 mRNA transcript.
To investigate whether these mouse PEG10 VLPs could incorporate unrelated RNAs, Segel et al.1 flanked a Cre recombinase coding sequence with Peg10 5′ and 3′ untranslated regions (UTRs), and co-transfected the construct together with PEG10 into Neuro2a mouse neuroblastoma cells. They also engineered the VLPs by adding the fusogen vesicular stomatitis virus envelope protein (VSVg) to facilitate cellular delivery. Strikingly, PEG10 VLPs with VSVg were secreted in extracellular vesicles and transferred the Cre mRNA into loxP–GFP cells (Fig. 1). This observation suggested that adding Peg10 UTRs to the mRNA cargo enables the PEG10 VLPs to transfer an mRNA of choice, and that the viral fusogenic protein is required for cell entry. Human PEG10, similarly to the mouse ortholog, could form VLPs and transfer mRNA.
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