![]() coli would be suited for production of VLP-based veterinary vaccines targeting livestock and companion animals where large amounts of doses must be produced at an affordable price.ĭownstream process Liquid chromatography Purification VLPs Virus-like particles.Ĭopyright © 2016 Elsevier B.V. The combination of this downstream strategy following production in E. ![]() The present study aims to characterize the structure and functional properties of this resin using bovine serum albumin (BSA, Mr65 kDa) and. The 3 steps purification protocol uses a recently developed multimodal size-exclusion chromatography medium (Capto™ Core 700) in combination with detergent extraction and size-exclusion polishing to reach a 89% VLP purity with a 19% yield. Capto Core 700 is a core-shell chromatographic support with an adsorbing core contained within an inert shell layer designed to purify larger biomolecules and bioparticles in a flow-through mode. Recombinant VLPs derived from the RNA bacteriophage MS2 displaying an epitope from the ectodomain of Matrix 2 protein from influenza A virus were produced and purified. In the present study we set up a size-exclusion chromatography-based, scalable purification protocol for the purification of a VLP-based influenza A vaccine produced in Escherichia coli. In particular, a rapid low cost purification process has been identified as a remaining key challenge in manufacturing process development. In recent years, the development of genetically engineered recombinant VLPs has accelerated the need for new, improved downstream processes. Several VLP-based vaccines are currently licensed and commercialized, and many vaccine candidates are now under preclinical and clinical studies. Size, oligomer assembly and repetitiveness of epitopes are optimal features to induce strong immune responses. Virus-like particles (VLPs) are promising molecular structures for the design and construction of novel vaccines, diagnostic tools, and gene therapy vectors.
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