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Cornelissen, J. J. L. M.

Publications and source records attributed to Cornelissen, J. J. L. M..

3 recordsLinked to original sources

Cowpea Chlorotic Mottle Virus virus-like particles as DNA or RNA delivery vehicle to fish cells

Cowpea Chlorotic Mottle Virus (CCMV) is an icosahedral plant virus composed of 180 monomeric units of the capsid protein. Virions encapsulate the viral RNA genome, which can be removed from the virion by changing pH conditions, after which the capsid proteins can be reversibly assembled to form empty CCMV virus-like particles (VLPs), or VLPs that have encapsulated either heterologous DNA or RNA. Earlier research has shown that CCMV VLPs are suitable as delivery vehicles for heterologous DNA/RNA molecules into mammalian cells, leading to subsequent expression of their encoded genes. In this study, we evaluated the potential of CCMV VLPs to encapsulate nucleic acids and transfer them to fish cells in vitro, and to zebrafish larvae and juveniles in vivo. VLPs containing pVax-GFP plasmid (3690 bp) were stable for up to 5 weeks in buffer at pH 7.2 and pH 5, whereas VLPs containing GFP-mRNA (1168 nt) were stable for up to 3 weeks, but only when stored in a buffer at pH 4.5. When administered directly to the culture medium, VLPs were readily taken up by fish as well as mammalian cell lines but could not unpack and transfer nucleic acids to the cells. VLPs delivered by transfection however, could transfer nucleic acids to the cells, leading to reporter gene expression. When VLPs were administered directly to the culture medium along with the cell-penetrating peptide dfTAT, only VLPs containing pVax-GFP in pH 7.2 buffer were able to transfer DNA to mammalian but not fish cells. In vivo however, upon intramuscular injection, the same VLPs were able to transfer plasmid DNA to myocytes of zebrafish larvae and juveniles as efficiently as when injecting naked plasmid DNA. Altogether, these findings provide the foundation for future studies on the use of CCMV VLPs as delivery vehicles for DNA or RNA to fish cells.

molecular biology↗

Folding of mRNA-DNA origami for controlled translation and viral vector packaging

mRNA is an important molecule in vaccine development and treatment of genetic disorders. Its capability to hybridize with DNA oligonucleotides in a programmable manner facilitates the formation of RNA-DNA origami structures, which can possess a well-defined morphology and serve as rigid supports for mRNA delivery. However, to date, compre- hensive studies on the requirements for efficient folding of mRNA into distinct mRNA-DNA structures while preserving its translation func- tionality remain elusive. Here, we systematically investigate the impact of design parameters on the folding of protein-encoding mRNA into mRNA-DNA origami structures and demonstrate the importance of the availability of ribosome-binding sequences on the translation effi- ciency. Furthermore, these hybrid structures can be encapsulated inside virus capsids for protecting them against nuclease degradation and also for enhancing their cellular uptake. This multicomponent system therefore showcases a modular and versatile nanocarrier. Our work pro- vides valuable insight into the design of mRNA-DNA origami structures contributing to the development of mRNA-based gene delivery platforms.

bioengineering↗

Introduction of Surface Loops as a Tool for Encapsulin Functionalization.

Encapsulin based protein cages are nanoparticles with different biomedical applications, such as targeted drug delivery or imaging agents. These particles are biocompatible and can be produced in bacteria, allowing large scale production and protein engineering. In order to use these bacterial nanocages in different applications, it is important to further explore the potential of their surface modification and optimize their production. In this study we design and show new surface modifications of the Thermotoga maritima (Tm) and Brevibacterium linens (Bl) encapsulins. Two new loops on Tm encapsulin with a His-tag insertion after the residue 64 and the residue 127, and the modification of the C-terminal on Bl encapsulin, are reported. The multi-modification of the Tm encapsulin enables up to 240 different functionalities on the cage surface, resulting from 4 potential modifications per protein subunit. We furthermore report an improved protocol giving a better stability and providing a notable increase of the production yield of the cages. Finally, we tested the stability of different encapsulin variants over a year and the results show a difference in stability arising from the tag insertion position. These first insights in the structure-property relationship of encapsulins, with respect to the position of a function loop, allow for further study of the use of these protein nanocages in biomedical applications. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=88 SRC="FIGDIR/small/444092v1_ufig1.gif" ALT="Figure 1"> View larger version (20K): org.highwire.dtl.DTLVardef@145a7a3org.highwire.dtl.DTLVardef@fb81org.highwire.dtl.DTLVardef@8012c7org.highwire.dtl.DTLVardef@51018b_HPS_FORMAT_FIGEXP M_FIG C_FIG

bioengineering↗