Promotion of self-nucleic acid fragments on the assembly of foot-and-mouth disease virus-like particles.

Haiyun Liu; Hu Dong; Ye Jin; Huichen Guo; Shiqi Sun

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Promotion of self-nucleic acid fragments on the assembly of foot-and-mouth disease virus-like particles.

Author: Haiyun LIU ¹ ; Hu DONG ¹ ; Ye JIN ¹ ; Huichen GUO ¹ ; Shiqi SUN ¹
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1. National Foot and Mouth Disease Reference Laboratory, State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, Gansu, China.
Publication Type:Journal Article
Keywords: 5′UTR; foot-and-mouth disease; internal ribosome entry site; size-exclusion chromatography; virus-like particles
MeSH: 5' Untranslated Regions; Capsid Proteins/metabolism*; Foot-and-Mouth Disease Virus/physiology*; Internal Ribosome Entry Sites; Nucleic Acids/metabolism*; Virus Assembly
From: Chinese Journal of Biotechnology 2020;36(10):2076-2082
CountryChina
Language:Chinese
Abstract: The special nucleic acid fragments, 5' untranslated region (5' UTR) and internal ribosome entry site (IRES) of foot-and-mouth disease virus (FMDV), which interact with the capsid proteins, were selected as scaffolds to investigate the assembly efficiency of foot-and-mouth disease (FMD) virus-like particles (VLPs). The assembled product was characterized by evaluation of particle size, surface potential, gel retardation assay, nuclease digestion experiments, size-exclusion chromatography, transmission electron microscopy and circular dichroism analysis. The results confirmed that the 5' UTR and IRES of FMDV co-assembled with the FMD VLPs and facilitated the assembly efficiency of FMD-VLPs. It demonstrates that the assembly efficiency of 75S particles of VLPs-5'UTR was significantly higher than those of the VLPs (P<0.001) and VLPs-IRES group (P<0.01). Comparatively the assembly efficiency of 12S particles of VLPs-IRES was significantly higher than those of the VLPs (P<0.000 1) and VLPs-5'UTR (P<0.000 1). It showed that the 5' UTR represented more effective in facilitating the assembly of VLPs. This study proposes an optimized strategy for improving the assembly efficiency of VLPs for the development of VLPs vaccine.