| Literature DB >> 33297420 |
Sun Young Park1,2, Jung-Min Lee1, Ah-Young Kim1, Sang Hyun Park1, Jae-Seok Kim1, Hyejin Kim1,2, Jung-Won Park1, Jong-Hyeon Park1, Young-Joon Ko1, Choi-Kyu Park2.
Abstract
Although polyethylene glycol (PEG) application is the most widely used method in removing nonstructural proteins (NSPs) for foot-and-mouth disease (FMD) vaccine production, some NSPs remaining in the antigen could elicit antibodies against these proteins after repeated vaccinations in livestock. Therefore, the purpose of this study was to purify the FMD virus (FMDV) via affinity chromatography using a heparin ligand to remove most proteins, including NSPs. Chromatography showed an intact virus (146S) particle recovery of 70% or more for three different strains of serotype O FMDV (two locally isolated strains and one genetically modified strain). The experimental vaccine made with antigens eluted via heparin affinity chromatography elicited virus-neutralizing antibodies against homologous viruses but did not induce antibodies against NSPs even after five immunizations in goats; this indicated that the NSPs were effectively removed from the vaccine antigen. This method can then be used to produce a higher-quality vaccine compared with PEG application in terms of the purity of the FMD vaccine. Therefore, this result would be an important groundwork for advanced FMD vaccine manufacturing in the near future.Entities:
Keywords: chromatography; foot-and-mouth disease virus; nonstructural protein; purification; vaccine
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Year: 2020 PMID: 33297420 PMCID: PMC7762290 DOI: 10.3390/v12121405
Source DB: PubMed Journal: Viruses ISSN: 1999-4915 Impact factor: 5.048