Novel expression and production of Foot-and-mouth disease virus vaccine candidates in Nicotiana benthamiana
type: CreativeWork
description: Foot-and-mouth disease, also known as FMD, is caused by the aphthovirus Foot-and-mouth disease virus (FMDV), which is a highly contagious disease of cloven-hoofed animals. It is endemic in Africa, parts of South America and southern Asia. In South Africa, the disease is controlled essentially through prophylactic vaccination. Current vaccines on the market are chemically inactivated virus strains. However, these are not considered ideal due to the possibly insufficient inactivation which could fail to render the virus harmless. Research on recombinant vaccines which obviate the need for high biosafety requirements for vaccine preparation has shown that recombinant FMDV virus-like particles (VLPs), devoid of viral genetic material, are an ideal vaccine candidate as they are as immunogenic as the virions themselves when administered to animals. These VLPs are formed by the assembly of the FMDV capsid proteins VP0, VP1 and VP3, which are generated upon the proteolytic cleavage of the capsid precursor protein P1-2A, by the FMDV 3C-protease. The expression platforms used to co-express and produce the component capsid proteins and the protease are usually mammalian, insect or E. coli cells. The use of these expression systems requires extensive bioreactor infrastructure and sterile conditions for vaccine preparation which are costly. In addition, some studies have shown how the co-expression of the 3C-protease can prove to be deleterious when expressed at a high concentration in expression systems. In order to circumvent this, and encourage more efficient production of the capsid proteins and subsequent VLP assembly, researchers have shown that the levels of the 3C-protease can be down-regulated by introducing mutations in the 3C gene or a ribosomal frameshift in the gene sequence which subsequently reduce its deleterious effect. Our laboratory has previously shown that similar FMDV VLPs can be assembled by the expression of FMDV P1-2A (referred to as oP1-2A, in this stud…
abstract: Foot-and-mouth disease, also known as FMD, is caused by the aphthovirus Foot-and-mouth disease virus (FMDV), which is a highly contagious disease of cloven-hoofed animals. It is endemic in Africa, parts of South America and southern Asia. In South Africa, the disease is controlled essentially through prophylactic vaccination. Current vaccines on the market are chemically inactivated virus strains. However, these are not considered ideal due to the possibly insufficient inactivation which could fail to render the virus harmless. Research on recombinant vaccines which obviate the need for high biosafety requirements for vaccine preparation has shown that recombinant FMDV virus-like particles (VLPs), devoid of viral genetic material, are an ideal vaccine candidate as they are as immunogenic as the virions themselves when administered to animals. These VLPs are formed by the assembly of the FMDV capsid proteins VP0, VP1 and VP3, which are generated upon the proteolytic cleavage of the capsid precursor protein P1-2A, by the FMDV 3C-protease. The expression platforms used to co-express and produce the component capsid proteins and the protease are usually mammalian, insect or E. coli cells. The use of these expression systems requires extensive bioreactor infrastructure and sterile conditions for vaccine preparation which are costly. In addition, some studies have shown how the co-expression of the 3C-protease can prove to be deleterious when expressed at a high concentration in expression systems. In order to circumvent this, and encourage more efficient production of the capsid proteins and subsequent VLP assembly, researchers have shown that the levels of the 3C-protease can be down-regulated by introducing mutations in the 3C gene or a ribosomal frameshift in the gene sequence which subsequently reduce its deleterious effect. Our laboratory has previously shown that similar FMDV VLPs can be assembled by the expression of FMDV P1-2A (referred to as oP1-2A, in this stud…
author: Veerapen, Varusha Pillay
language: eng
date published: 2017
date modified: 2026-07-22T22:22:51Z
provider: University of Cape Town
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Department of Molecular and Cell Biology

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property ID: Handle
value: http://hdl.handle.net/11427/27240