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OVs implement a unique mode of action, tumor-restricted viral infection, replication, cell lysis and spread. In contrast to gene therapy where a virus is used as a mere carrier for transgene delivery, OV therapy uses the virus itself as an active ingredient. OVs are genetically engineered or naturally occurring viruses that can selectively replicate in and kill cancer cells without, or at least to a less extent, harming benign tissues. Virus particles find also application in oncolytic virus (OV) therapy, which has been recognized as a promising and potentially break-through therapeutic approach for cancer treatment.
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Therefore, there exists an ongoing need to provide suitable vaccines having an acceptable immunogenicity, safety and tolerability profile for vaccination. The major hallmarks to be fulfilled by a vaccine candidate based on a virus or viral component are its safety, purity and potency. The WHO and the responsible national and regional approval authorities, like the FDA or the EMEA, understandably impose high product and labelling requirements to a composition comprising a virus material used as vaccine or therapeutic to achieve the provision of safe biological products. Regulatory agencies demand the provision of specifically produced virus material to guarantee the safety of the respective material.
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Virus particles are used in a variety of different prophylactic and curative medical applications, e.g., for vaccination as well as for therapeutic purposes. large and pleomorphic, virus particles, particularly measles viruses (MVs) and more particularly viruses having a MV scaffold to yield fractions or compositions comprising virus particles in high yield and low content of impurities such as host cell DNA contaminants and/or host cell protein contaminants. A mechanistic model is developed to describe the adsorption kinetics in these particles and can be used to predict and optimize the flow-through purification of viral vaccines and other large therapeutic bioparticles.The present invention generally relates to the field of virology and specifically relates to chromatography based purification strategies of sterically demanding, i.e. However, some of this advantage is lost if the feed is a mixture of BSA and Tg since, in this case, Tg binding leads to greater diffusional hindrance for BSA. Column measurements show that, despite the higher static capacity of Capto Core 400 for BSA, the dynamic binding capacity is greater for Capto Core 700 due to its faster kinetics.
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Adsorbed Tg further hinders the diffusion of BSA in both resins. Mass transfer in both resins is affected by diffusional resistances through the shell and within the adsorbing core. However, for the much larger Tg, the attainable capacity is substantially larger for Capto Core 700. The BSA binding capacity of Capto Core 400 is approximately double that of Capto Core 700 due to the smaller pores and higher surface area of the former resin. Although shell thicknesses are comparable, the two resins differ substantially in pore size (pore radii of 19 and 50 nm, respectively). Structural and functional characteristics of the two resins Capto Core 400 and 700 are compared using bovine serum albumin (BSA) and thyroglobulin (Tg) as models for small and large protein contaminants. These resins are useful for the flow-through purification of bioparticles such as viruses, viral vectors, and extracellular vesicles. Both resins are agarose-based and contain an adsorbing core surrounded by an inert shell, which prevents the binding of larger particles. Capto TM Core 400 and 700 resins are core-shell chromatographic media that combine size exclusion and multimodal anion exchange characteristics.