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ABSTRACT: Background
Inactivated vaccines are limited in preventing foot-and-mouth disease (FMD) due to safety problems. Recombinant virus-like particles (VLPs) are an excellent candidate for a novel vaccine for preventing FMD, given that VLPs have similar immunogenicity as natural viruses and are replication- and infection-incompetent.Objectives
The 3C protease and P1 polyprotein of type O FMD virus (FDMV) was expressed in yeast Hansenula polymorpha to generate self-resembling VLPs, and the potential of recombinant VLPs as an FMD vaccine was evaluated.Methods
BALB/c mice were immunized with recombinant purified VLPs using CpG oligodeoxynucleotide and aluminum hydroxide gel as an adjuvant. Cytokines and lymphocytes from serum and spleen were analyzed by enzyme-linked immunosorbent assay, enzyme-linked immunospot assay, and flow cytometry.Results
The VLPs of FMD were purified successfully from yeast protein with a diameter of approximately 25 nm. The immunization of mice showed that animals produced high levels of FMDV antibodies and a higher level of antibodies for a longer time. In addition, higher levels of interferon-γ and CD4+ T cells were observed in mice immunized with VLPs.Conclusions
The expression of VLPs of FMD in H. polymorpha provides a novel strategy for the generation of the FMDV vaccine.
SUBMITTER: Zhang J
PROVIDER: S-EPMC9899949 | biostudies-literature | 2023 Jan
REPOSITORIES: biostudies-literature
Zhang Jianhui J Ge Jun J Li Juyin J Li Jianqiang J Zhang Yong Y Shi Yinghui Y Sun Jiaojiao J Wang Qiongjin Q Zhang Xiaobo X Zhao Xingxu X
Journal of veterinary science 20230101 1
<h4>Background</h4>Inactivated vaccines are limited in preventing foot-and-mouth disease (FMD) due to safety problems. Recombinant virus-like particles (VLPs) are an excellent candidate for a novel vaccine for preventing FMD, given that VLPs have similar immunogenicity as natural viruses and are replication- and infection-incompetent.<h4>Objectives</h4>The 3C protease and P1 polyprotein of type O FMD virus (FDMV) was expressed in yeast <i>Hansenula polymorpha</i> to generate self-resembling VLPs ...[more]