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• W4313679547 endingPage "106231" @default.
• W4313679547 startingPage "106231" @default.
• W4313679547 abstract "Recombinant virus-like particles (VLP) with single capsid protein have been successfully produced through prokaryotic system, but for those with multiple capsid proteins such as the foot-and-mouth disease virus (FMDV), this approach is more challenging. In this study, in vitro assembly of FMDV VLP was investigated with its capsids VP1, VP2 and VP3 separately expressed as inclusion bodies. After extraction and solubilization, three capsids were purified in denatured state through a flow-through model, increasing its purity to 90%. VLP assembly for FMDV was observed after diluting the mixture of denatured capsids in the ration of 1: 1: 1, while no VLP appeared if the separately diluted and refolded capsids were co-incubated. This result suggests certain synergetic interactions exist among the three capsids, which are crucial for FMDV VLP assembly. Sodium chloride and capsid protein concentration both greatly affect the assembling efficiency. After purification through size exclusion chromatography, VLP with similar diameter and morphology as inactivated FMDV were obtained, which elicited high IgG titers and B cell activation when vaccinated in mouse. It could also induce specific humoral and cellular immune responses in splenocytes proliferative experiments. Our study demonstrated the feasibility of in vitro assembling FMDV VLP from inclusion bodies of VP1, VP2 and VP3 for the first time." @default.
• W4313679547 created "2023-01-08" @default.
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• W4313679547 date "2023-04-01" @default.
• W4313679547 modified "2023-09-26" @default.
• W4313679547 title "Synergetic interaction of capsid proteins for virus-like particles assembly of foot-and-mouth disease virus (serotype O) from the inclusion bodies" @default.
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• W4313679547 doi "https://doi.org/10.1016/j.pep.2023.106231" @default.
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• W4313679547 hasPublicationYear "2023" @default.
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