Expression of Foot-and-Mouth Disease Virus Epitope by a Bamboo Mosaic Virus-Based Vector

碩士 === 國立中興大學 === 生物科技學研究所 === 92 === Foot-and-mouth disease virus (FMDV) is a constant threat to domestic livestock throughout the world. The outbreak of FMD has led to huge economic loss in affected countries. The conventional vaccine against FMDV is based on the chemically inactivated...

Full description

Bibliographic Details
Main Authors: Ming-Yu Lin, 林銘裕
Other Authors: Yau-Heiu Hsu
Format: Others
Language:zh-TW
Published: 2004
Online Access:http://ndltd.ncl.edu.tw/handle/63303529825776193373
Description
Summary:碩士 === 國立中興大學 === 生物科技學研究所 === 92 === Foot-and-mouth disease virus (FMDV) is a constant threat to domestic livestock throughout the world. The outbreak of FMD has led to huge economic loss in affected countries. The conventional vaccine against FMDV is based on the chemically inactivated virus. This remains a potential risk of virus escape by biosecurity failure or incomplete viral inactivation. Therefore, alternative approaches to produce an efficient and safe FMDV vaccine are needed to circumvent the use of inactivated virus. Development of plant virus-based vaccines has several advantages, such as easy to produce, low cost and safe. Advances in understanding the mechanism of immune response in molecular level have led to the successful design and production of FMDV vaccines using different expression systems. The prominent G—H loop of the VP 1 capsid protein of FMDV spanning residues 134—158 has been identified as a major immunogenic site for eliciting neutralizing antibodies and has formed the basis for the peptide approach to vaccination. Bamboo mosaic virus (BaMV), a member of the potexvirus, is a single-stranded, positive-sense RNA virus with a genome size about 6.4 kb which contains five conserved open reading frame (ORFs). In this study, the immunogenic dominant epitope of FMDV was expressed in Chenopodium quinoa using a vector based on a recombinant Bamboo mosaic virus (BaMV). The recombinant virus BS-FMDV-VP1128164-Nd35mcp (Vd35mCP) contains 37 amino acid residues from G-H loop fused to the amino terminus of BaMV capsid protein (CP). Vd35mCP infected C. quinoa produced large quantity of stable progeny viral particles assembled with the modified CP subunits. Mice and guinea pigs were used to test the immunogenic effects of the recombinant virus. All mice produce high serum tilter after parenteral injection with different dose of Vd35mCP, or the overexpressed VP1 protein in E. coli. However, oral administration of the Vd35mCP to guinea pigs cannot elite high serum IgG against FMDV, which remains further investigation.